Polypeptides having xanthan degrading activity and polynucleotides encoding same

ABSTRACT

The present invention relates to isolated polypeptides having xanthan degrading activity, catalytic domains and polynucleotides encoding the polypeptides and catalytic domains. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides and catalytic domains.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a 35 U.S.C. 371 national application ofPCT/EP2013/059472 filed May 7, 2013, which claims priority or thebenefit under 35 U.S.C. 119 of European application nos. 12167023.6 and13150833.5 filed May 7, 2012 and Jan. 10, 2013, respectively, and U.S.provisional application Nos. 61/644,033 and 61/754,663 and filed May 8,2012 and Jan. 21, 2013, respectively. The contents of each applicationare fully incorporated herein by reference.

REFERENCE TO A SEQUENCE LISTING

This application contains a Sequence Listing in computer readable form,which is incorporated herein by reference.

BACKGROUND OF THE INVENTION

1. Field of the Invention

The present invention relates to polypeptides having xanthan degradingactivity, in particular xanthan lyase activity and to GH9 endoglucanaseshaving activity on xanthan gum pretreated with xanthan lyase, catalyticdomains, and polynucleotides encoding the polypeptides and catalyticdomains. The invention also relates to nucleic acid constructs, vectors,and host cells comprising the polynucleotides as well as methods ofproducing and using the polypeptides and catalytic domains. Theinvention further relates to compositions comprising GH9 endoglucanasesand/or xanthan lyases for use in detergents and in the drilling and oilindustries.

2. Description of the Related Art

Xanthan gum is a polysaccharide derived from the bacterial coat ofXanthomonas campestris. It is produced by the fermentation of glucose,sucrose, or lactose by the Xanthomonas campestris bacterium. After afermentation period, the polysaccharide is precipitated from a growthmedium with isopropyl alcohol, dried, and ground into a fine powder.Later, it is added to a liquid medium to form the gum.

Xanthan gum is a natural polysaccharide consisting of different sugarswhich are connected by several different bonds, such asβ-D-mannosyl-β-D-1,4-glucuronosyl bonds andβ-D-glucosyl-β-D-1,4-glucosyl bonds. Xanthan gum is at least partlysoluble in water and forms highly viscous solutions or gels.

Complete enzymatic degradation of xanthan gum requires several enzymaticactivities including xanthan lyase activity and endo-β-1,4-glucanaseactivity. Xanthan lyases are enzymes that cleave theβ-D-mannosyl-β-D-1,4-glucuronosyl bond of xanthan and have beendescribed in the literature. Xanthan degrading enzymes are known in theart e.g. have two xanthan lyases been isolated from Paenibacillusalginolyticus XL-1 (e.g. Ruijssenaars et al. (1999) ‘A pyruvatedmannose-specific xanthan lyase involved in xanthan degradation byPaenibacillus alginolyticus XL-1’, Appl. Environ. Microbiol. 65(6):2446-2452, and Ruijssenaars et al. (2000), ‘A novel gene encodingxanthan lyase of Paenibacillus alginolyticus strain XL-1’, Appl.Environ. Microbiol. 66(9): 3945-3950).

Glycoside hydrolases are enzymes that catalyse the hydrolysis of theglycosyl bond to release smaller sugars. There are over 100 classes ofglycoside hydrolases which have been classified, see Henrissat et al.(1991) ‘A classification of glycosyl hydrolases based on amino-acidsequence similarities’, J. Biochem. 280: 309-316 and the Uniprot websiteat www.cazy.org. The glycoside hydrolase family 9 (GH9) consists of over70 different enzymes that are mostly endoglucanases (EC 3.2.1.4),cellobiohydrolases (EC 3.2.1.91), β-glucosidases (EC 3.2.1.21) andexo-β-glucosaminidase (EC 3.2.1.165). A GH9 from Microbacteriumtestaceum StLB037 having 84.5% sequence identity to SEQ ID NO: 12, 79.1%sequence identity to SEQ ID NO: 10 and 74.0% sequence identity to SEQ IDNO: 14 has been published by T. Morohoshi et al, (2011) J. Bacteriol.193(8), 2072-2073.

In recent years xanthan gum has been use as an ingredient in manyconsumer products including foods (e.g. as thickening agent in salatdressings and dairy products) and cosmetics (e.g. as stabilizer andthickener in toothpaste and make-up to prevent ingredients fromseparating) and cosmetics (such as sun creams). Further xanthan gum hasfound use in the oil industry as well as an additive to regulate theviscosity of drilling fluids etc. The widespread use of xanthan gum hasled to a desire to degrade solutions or gels of xanthan gum therebyallowing easier removal of the byproducts. It has been suggested to adda xanthan lyase to a detergent composition in order to remove xanthangum containing stains, e.g. in EP0896998A, but this publication does notcontain any experimental data demonstrating any effect thereof.

The invention provides new and improved enzymes for the degradation ofxanthan gum and the use of such enzymes for cleaning purposes, such asthe removal of xanthan gum stains, and in the drilling and oilindustries.

SUMMARY OF THE INVENTION

In one aspect the invention relates to an isolated GH9 endoglucanasehaving activity on xanthan gum pretreated with xanthan lyase, selectedfrom the group consisting of:

-   -   (a) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        2;    -   (b) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        10;    -   (c) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        12;    -   (d) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        14;    -   (e) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        48;    -   (f) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        52;    -   (g) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        56;    -   (h) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        82;    -   (i) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        86;    -   (j) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        90;    -   (k) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        94;    -   (l) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        98;    -   (m) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        102;    -   (n) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        130;    -   (o) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        134;    -   (p) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        138;    -   (q) a polypeptide encoded by a polynucleotide that hybridizes        under medium stringency conditions, medium-high stringency        conditions, high stringency conditions, or very high stringency        conditions with:        -   (i) the mature polypeptide coding sequence of SEQ ID NO: 1;        -   (ii) the mature polypeptide coding sequence of SEQ ID NO: 9;        -   (iii) the mature polypeptide coding sequence of SEQ ID NO:            11;        -   (iv) the mature polypeptide coding sequence of SEQ ID NO:            13;        -   (v) the mature polypeptide coding sequence of SEQ ID NO: 47;        -   (vi) the mature polypeptide coding sequence of SEQ ID NO:            51;        -   (vii) the mature polypeptide coding sequence of SEQ ID NO:            55;        -   (viii) the mature polypeptide coding sequence of SEQ ID NO:            81;        -   (ix) the mature polypeptide coding sequence of SEQ ID NO:            85;        -   (x) the mature polypeptide coding sequence of SEQ ID NO: 89;        -   (xi) the mature polypeptide coding sequence of SEQ ID NO:            93;        -   (xii) the mature polypeptide coding sequence of SEQ ID NO:            97;        -   (xiii) the mature polypeptide coding sequence of SEQ ID NO:            101;        -   (xiv) the mature polypeptide coding sequence of SEQ ID NO:            129;        -   (xv) the mature polypeptide coding sequence of SEQ ID NO:            133;        -   (xvi) the mature polypeptide coding sequence of SEQ ID NO:            137; or        -   (xvii) the full-length complement thereof of (i), (ii),            (iii), (iv), (v), (vi), (vii), (viii), (ix), (x), (xi),            (xii), (xiii), (xiv), (xv), or (xvi);    -   (r) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 1;    -   (s) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 9;    -   (t) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 11;    -   (u) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 13;    -   (v) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 47;    -   (w) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 51;

(x) a polypeptide encoded by a polynucleotide having at least 80%, e.g.,at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100% sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 55;

-   -   (y) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 81;    -   (z) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 85;    -   (aa) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 89;    -   (ab) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 93;    -   (ac) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 97;    -   (ad) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 101;    -   (ae) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 129;    -   (af) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 133;    -   (ag) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 137;    -   (ah) a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID        NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 48, SEQ ID NO:        52, SEQ ID NO: 56, SEQ ID NO: 82, SEQ ID NO: 86, SEQ ID NO: 90,        SEQ ID NO: 94, SEQ ID NO: 98, SEQ ID NO: 102, SEQ ID NO: 130,        SEQ ID NO: 134 or SEQ ID NO: 138 comprising a substitution,        deletion, and/or insertion at one or more positions (e.g.        several); and    -   (ai) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q), (r),        (s), (t), (u), (v), (w), (x), (y), (z), (aa), (ab), (ac), (ad),        (ae), (af), (ag) or (ah) that has activity on xanthan gum        pretreated with xanthan lyase, xanthan degrading activity and/or        endo-β-1,4-glucanase activity.

In another aspect, the invention relates to an isolated polypeptidehaving xanthan lyase activity selected from the group consisting of:

-   -   (a) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        4;    -   (b) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        46;    -   (c) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        60;    -   (d) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        64;    -   (e) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        106;    -   (f) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        110;    -   (g) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        114;    -   (h) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        118;    -   (i) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        122;    -   (j) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        126;    -   (k) a polypeptide encoded by a polynucleotide that hybridizes        under medium stringency conditions, medium-high stringency        conditions, high stringency conditions, or very high stringency        conditions with:        -   (i) the mature polypeptide coding sequence of SEQ ID NO: 3;        -   (ii) the mature polypeptide coding sequence of SEQ ID NO:            45;        -   (iii) the mature polypeptide coding sequence of SEQ ID NO:            59;        -   (iv) the mature polypeptide coding sequence of SEQ ID NO:            63;        -   (v) the mature polypeptide coding sequence of SEQ ID NO:            105;        -   (vi) the mature polypeptide coding sequence of SEQ ID NO:            109;        -   (vii) the mature polypeptide coding sequence of SEQ ID NO:            113;        -   (viii) the mature polypeptide coding sequence of SEQ ID NO:            117;        -   (ix) the mature polypeptide coding sequence of SEQ ID NO:            121;        -   (x) the mature polypeptide coding sequence of SEQ ID NO:            125; or        -   (xi) the full-length complement thereof of (i), (ii), (iii),            (iv), (v), (vi), (vii), (viii), (ix), or (x);    -   (l) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 3;    -   (m) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 45;    -   (n) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 59;    -   (o) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 63;    -   (p) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 105;    -   (q) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 109;    -   (r) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 113;    -   (s) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 117;    -   (t) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 121,    -   (u) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 125;    -   (v) a variant of the mature polypeptide of SEQ ID NO: 4, SEQ ID        NO: 46, SEQ ID NO: 60, SEQ ID NO: 64, SEQ ID NO: 106, SEQ ID NO:        110, SEQ ID NO: 114, SEQ ID NO: 118, SEQ ID NO: 122 or SEQ ID        NO: 126 comprising a substitution, deletion, and/or insertion at        one or more positions (e.g. several); and    -   (w) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q), (r),        (s), (t), (u) or (v) that has xanthan lyase activity.

In another aspect, the invention relates to a composition comprising anisolated GH9 endoglucanase having activity on xanthan gum pretreatedwith xanthan lyase, according to the invention. In a further aspect, thecomposition further comprises an isolated polypeptide having xanthanlyase activity according to the invention. The composition of theinvention is preferably a detergent composition comprising one or moredetergent components or a composition for degrading xanthan gum.

It has surprisingly been found that the a composition comprising axanthan lyase and a GH9 endoglucanase having activity on xanthan gumpretreated with xanthan lyase is significantly more efficient indegrading xanthan gum than would have been expected based on theactivity of the individual enzymes.

The present invention also relates to isolated polynucleotides encodingthe polypeptides of the present invention; nucleic acid constructs;recombinant expression vectors; recombinant host cells comprising thepolynucleotides; and methods of producing the polypeptides.

The present invention further relates to the use of the composition ofthe invention for degrading xanthan gum, for washing or cleaningtextiles and/or hard surfaces, such as dish wash, wherein thecomposition has an enzyme detergency benefit, or for controlling theviscosity of drilling fluids. The invention also relates to methods ofdegrading xanthan gum, wherein xanthan gum is on the surface of a hardsurface or textile, wherein xanthan gum is used in fracturing of asubterranean formation perpetrated by a well bore, or wherein thexanthan gum is a component in borehole filtercake.

OVERVIEW OF SEQUENCE LISTING

SEQ ID NO: 1 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Paenibacillus sp NN062047.

SEQ ID NO: 2 is the amino acid sequence as deduced from SEQ ID NO: 1.

SEQ ID NO: 3 is the truncated DNA sequence of the xanthan lyase asisolated from Paenibacillus sp NN018054.

SEQ ID NO: 4 is the amino acid sequence as deduced from SEQ ID NO: 3.

SEQ ID NO: 5 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 1 operably linked with a His-tag.

SEQ ID NO: 6 is the amino acid sequence as deduced from SEQ ID NO: 5.

SEQ ID NO: 7 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 3 operably linked with a His-tag.

SEQ ID NO: 8 is the amino acid sequence as deduced from SEQ ID NO: 7.

SEQ ID NO: 9 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Microbacterium sp NN062149.

SEQ ID NO: 10 is the amino acid sequence as deduced from SEQ ID NO: 9.

SEQ ID NO: 11 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Microbacterium sp NN062148.

SEQ ID NO: 12 is the amino acid sequence as deduced from SEQ ID NO: 11.

SEQ ID NO: 13 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Microbacterium sp NN062045.

SEQ ID NO: 14 is the amino acid sequence as deduced from SEQ ID NO: 13.

SEQ ID NO: 15 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 9 operably linked with a His-tag.

SEQ ID NO: 16 is the amino acid sequence as deduced from SEQ ID NO: 15.

SEQ ID NO: 17 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 11 operably linked with a His-tag.

SEQ ID NO: 18 is the amino acid sequence as deduced from SEQ ID NO: 17.

SEQ ID NO: 19 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 13 operably linked with a His-tag.

SEQ ID NO: 20 is the amino acid sequence as deduced from SEQ ID NO: 19.

SEQ ID NO: 21 is Primer D88F.

SEQ ID NO: 22 is Primer D89R.

SEQ ID NO: 23 is Primer D124F.

SEQ ID NO: 24 is Primer D125R.

SEQ ID NO: 25 is Primer D126F.

SEQ ID NO: 26 is Primer D127R.

SEQ ID NO: 27 is Primer D128F.

SEQ ID NO: 28 is Primer D129R.

SEQ ID NO: 29 is the DNA sequence of the Savinase signal peptide.

SEQ ID NO: 30 is the His-Tag (also called poly-histidine tag).

SEQ ID NO: 31 is Primer D117F.

SEQ ID NO: 32 is Primer D118R.

SEQ ID NO: 33 is Primer D158F.

SEQ ID NO: 34 is Primer D159R.

SEQ ID NO: 35 is Primer D168F.

SEQ ID NO: 36 is Primer D169R.

SEQ ID NO: 37 is Primer D170F.

SEQ ID NO: 38 is Primer D170R.

SEQ ID NO: 39 is Primer D171F.

SEQ ID NO: 40 is Primer D172R.

SEQ ID NO: 41 is Primer D160F.

SEQ ID NO: 42 is Primer D161R.

SEQ ID NO: 43 is Primer F-C3AQX.

SEQ ID NO: 44 is Primer R-C3AQX.

SEQ ID NO: 45 is the full length DNA sequence of the xanthan lyase asisolated from Paenibacillus sp NN018054.

SEQ ID NO: 46 is the amino acid sequence as deduced from SEQ ID NO: 45.

SEQ ID NO: 47 is the DNA sequence of the truncated GH9 endoglucanase asisolated from Paenibacillus sp NN062047

SEQ ID NO: 48 is the amino acid sequence as deduced from SEQ ID NO: 47.

SEQ ID NO: 49 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 47 operably linked with a His-tag.

SEQ ID NO: 50 is the amino acid sequence as deduced from SEQ ID NO: 49.

SEQ ID NO: 51 is the DNA sequence of the truncated GH9 endoglucanase asisolated from Paenibacillus sp NN062047.

SEQ ID NO: 52 is the amino acid sequence as deduced from SEQ ID NO: 51.

SEQ ID NO: 53 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 51 operably linked with a His-tag.

SEQ ID NO: 54 is the amino acid sequence as deduced from SEQ ID NO: 53.

SEQ ID NO: 55 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Paenibacillus sp NN062253.

SEQ ID NO: 56 is the amino acid sequence as deduced from SEQ ID NO: 55

SEQ ID NO: 57 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 55 operably linked with a His-tag.

SEQ ID NO: 58 is the amino acid sequence as deduced from SEQ ID NO: 57.

SEQ ID NO: 59 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062250.

SEQ ID NO: 60 is the amino acid sequence as deduced from SEQ ID NO: 59.

SEQ ID NO: 61 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 59 operably linked with a His-tag.

SEQ ID NO: 62 is the amino acid sequence as deduced from SEQ ID NO: 61.

SEQ ID NO: 63 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062047.

SEQ ID NO: 64 is the amino acid sequence as deduced from SEQ ID NO: 63.

SEQ ID NO: 65 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 63 operably linked with a His-tag.

SEQ ID NO: 66 is the amino acid sequence as deduced from SEQ ID NO: 65.

SEQ ID NO: 67 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 45 operably linked with a His-tag.

SEQ ID NO: 68 is the amino acid sequence as deduced from SEQ ID NO: 67.

SEQ ID NO: 69 is Primer D244F.

SEQ ID NO: 70 is Primer D245R.

SEQ ID NO: 71 is Primer D242F.

SEQ ID NO: 72 is Primer D243R.

SEQ ID NO: 73 is Primer D271F.

SEQ ID NO: 74 is Primer D272R.

SEQ ID NO: 75 is Primer D289F.

SEQ ID NO: 76 is Primer D290R.

SEQ ID NO: 77 is Primer D293F.

SEQ ID NO: 78 is Primer D294R.

SEQ ID NO: 79 is Primer D332F.

SEQ ID NO: 80 is Primer D333R.

SEQ ID NO: 81 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Paenibacillus sp NN062046.

SEQ ID NO: 82 is the amino acid sequence as deduced from SEQ ID NO: 81.

SEQ ID NO: 83 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 81 operably linked with a His-tag.

SEQ ID NO: 84 is the amino acid sequence as deduced from SEQ ID NO: 83.

SEQ ID NO: 85 is the DNA sequence of the truncated GH9 endoglucanase asisolated from Paenibacillus sp NN018054.

SEQ ID NO: 86 is the amino acid sequence as deduced from SEQ ID NO: 85.

SEQ ID NO: 87 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 85.

SEQ ID NO: 88 is the amino acid sequence as deduced from SEQ ID NO: 87.

SEQ ID NO: 89 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Paenibacillus sp NN062408.

SEQ ID NO: 90 is the amino acid sequence as deduced from SEQ ID NO: 89.

SEQ ID NO: 91 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 89.

SEQ ID NO: 92 is the amino acid sequence as deduced from SEQ ID NO: 91.

SEQ ID NO: 93 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Paenibacillus sp NN018054.

SEQ ID NO: 94 is the amino acid sequence as deduced from SEQ ID NO: 93.

SEQ ID NO: 95 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 93 operably linked with a His-tag.

SEQ ID NO: 96 is the amino acid sequence as deduced from SEQ ID NO: 95.

SEQ ID NO: 97 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Paenibacillus sp NN062332.

SEQ ID NO: 98 is the amino acid sequence as deduced from SEQ ID NO: 97.

SEQ ID NO: 99 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 97 operably linked with a His-tag.

SEQ ID NO: 100 is the amino acid sequence as deduced from SEQ ID NO: 99.

SEQ ID NO: 101 is the DNA sequence of the GH9 endoglucanase as isolatedfrom Microbacterium testaceum.

SEQ ID NO: 102 is the amino acid sequence as deduced from SEQ ID NO:101.

SEQ ID NO: 103 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 101 operably linked with a His-tag.

SEQ ID NO: 104 is the amino acid sequence as deduced from SEQ ID NO:103.

SEQ ID NO: 105 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062147.

SEQ ID NO: 106 is the amino acid sequence as deduced from SEQ ID NO:105.

SEQ ID NO: 107 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 105 operably linked with a His-tag.

SEQ ID NO: 108 is the amino acid sequence as deduced from SEQ ID NO:107.

SEQ ID NO: 109 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062193.

SEQ ID NO: 110 is the amino acid sequence as deduced from SEQ ID NO:109.

SEQ ID NO: 111 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 109 operably linked with a His-tag.

SEQ ID NO: 112 is the amino acid sequence as deduced from SEQ ID NO:111.

SEQ ID NO: 113 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062408.

SEQ ID NO: 114 is the amino acid sequence as deduced from SEQ ID NO:113.

SEQ ID NO: 115 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 113 operably linked with a His-tag.

SEQ ID NO: 116 is the amino acid sequence as deduced from SEQ ID NO:115.

SEQ ID NO: 117 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062332.

SEQ ID NO: 118 is the amino acid sequence as deduced from SEQ ID NO:117.

SEQ ID NO: 119 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 117 operably linked with a His-tag.

SEQ ID NO: 120 is the amino acid sequence as deduced from SEQ ID NO:119.

SEQ ID NO: 121 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062046.

SEQ ID NO: 122 is the amino acid sequence as deduced from SEQ ID NO:121.

SEQ ID NO: 123 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 121 operably linked with a His-tag.

SEQ ID NO: 124 is the amino acid sequence as deduced from SEQ ID NO:123.

SEQ ID NO: 125 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062253.

SEQ ID NO: 126 is the amino acid sequence as deduced from SEQ ID NO:125.

SEQ ID NO: 127 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 125 operably linked with a His-tag.

SEQ ID NO: 128 is the amino acid sequence as deduced from SEQ ID NO:127.

SEQ ID NO: 129 is the DNA sequence of the xanthan lyase as isolated fromMicrobacterium sp NN062175.

SEQ ID NO: 130 is the amino acid sequence as deduced from SEQ ID NO:129.

SEQ ID NO: 131 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 129 operably linked with a His-tag.

SEQ ID NO: 132 is the amino acid sequence as deduced from SEQ ID NO:131.

SEQ ID NO: 133 is the DNA sequence of the xanthan lyase as isolated fromPaenibacillus sp NN062193.

SEQ ID NO: 134 is the amino acid sequence as deduced from SEQ ID NO:133.

SEQ ID NO: 135 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 133 operably linked with a His-tag.

SEQ ID NO: 136 is the amino acid sequence as deduced from SEQ ID NO:135.

SEQ ID NO: 137 is the DNA sequence of the truncated xanthan lyase asisolated from Paenibacillus sp NN062193.

SEQ ID NO: 138 is the amino acid sequence as deduced from SEQ ID NO:137.

SEQ ID NO: 139 is the DNA sequence of the recombinant expressed sequencefrom SEQ ID NO: 137 operably linked with a His-tag.

SEQ ID NO: 140 is the amino acid sequence as deduced from SEQ ID NO:139.

SEQ ID NO: 141 is Primer F-0597B.

SEQ ID NO: 142 is Primer R-0597B.

SEQ ID NO: 143 is Primer F-05B9G.

SEQ ID NO: 144 is Primer R-05B9G.

SEQ ID NO: 145 is Primer F-059T2.

SEQ ID NO: 146 is Primer R-059T2.

SEQ ID NO: 147 is Primer F-C4AM9.

SEQ ID NO: 148 is Primer R-C4AM9.

SEQ ID NO: 149 is Primer F-C4AKF.

SEQ ID NO: 150 is Primer R-C4AKF.

SEQ ID NO: 151 is Primer F-059TM.

SEQ ID NO: 152 is Primer R-059TM.

SEQ ID NO: 153 is Primer F-059SY.

SEQ ID NO: 154 is Primer R-059SY.

SEQ ID NO: 155 is Primer F-C3AX4.

SEQ ID NO: 156 is Primer R-C3AX4.

SEQ ID NO: 157 is Primer F-C4AKA.

SEQ ID NO: 158 is Primer R-C4AKA.

SEQ ID NO: 159 is Primer F-C3BXT.

SEQ ID NO: 160 is Primer R-C3BXT.

SEQ ID NO: 161 is Primer F-0597E.

SEQ ID NO: 162 is Primer R-0597E.

SEQ ID NO: 163 is Primer F-0597F.

SEQ ID NO: 164 is Primer R-0597F.

SEQ ID NO: 165 is Primer F-C3FCE.

SEQ ID NO: 166 is Primer R-C3FCE.

SEQ ID NO: 167 is Primer D14KMG.

SEQ ID NO: 168 is Primer D14KMH.

SEQ ID NO: 169 is Primer D14N38.

SEQ ID NO: 170 is Primer D14N39.

Identity Matrix of GH9 Endoglucanase Sequences

SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID NO: 2 NO:10 NO: 12 NO: 14 NO: 48 NO: 52 NO: 56 NO: 82 NO: 86 SEQ 2 100 51.3 49.950.0 62.7 64.7 81.2 51.6 55.5 SEQ 10 51.3 100 78.7 78.3 47.9 47.9 51.754.1 52.1 SEQ 12 49.9 78.7 100 74.3 48.4 48.4 50.8 53.6 52.6 SEQ 14 50.078.3 74.3 100 48.4 48.4 50.8 51.3 52.3 SEQ 48 62.7 47.9 48.4 48.4 100100 62.0 54.4 56.1 SEQ 52 64.7 47.9 48.4 48.4 100 100 64.8 55.4 56.1 SEQ56 81.2 51.7 50.8 50.8 62.0 64.8 100 53.2 56.1 SEQ 82 51.6 54.1 53.651.3 54.4 55.4 53.2 100 70.5 SEQ 86 55.5 52.1 52.6 52.3 56.1 56.1 56.170.5 100 SEQ 90 49.7 52.0 51.6 53.2 49.4 51.9 52.3 63.5 66.8 SEQ 94 53.952.1 52.6 52.3 54.1 56.1 54.5 69.8 100 SEQ 98 53.4 52.8 53.4 52.8 54.556.7 54.0 69.9 73.1 SEQ 48.5 79.3 84.6 74.2 48.5 48.5 50.0 53.7 51.9 102SEQ 50.7 78.9 99.7 74.4 48.4 48.4 51.0 53.9 52.8 130 SEQ 52.9 52.6 53.453.5 53.9 56.5 53.0 66.4 68.4 134 SEQ 56.2 52.6 53.4 53.5 56.3 56.5 56.366.6 68.2 138 SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID NO: 90NO: 94 NO: 98 NO: 102 NO: 130 NO: 134 NO: 138 SEQ 2 49.7 53.9 53.4 48.550.7 52.9 56.2 SEQ 10 52.0 52.1 52.8 79.3 78.9 52.6 52.6 SEQ 12 51.652.6 53.4 84.6 99.7 53.4 53.4 SEQ 14 53.2 52.3 52.8 74.2 74.4 53.5 53.5SEQ 48 49.4 54.1 54.5 48.5 48.4 53.9 56.3 SEQ 52 51.9 56.1 56.7 48.548.4 56.5 56.5 SEQ 56 52.3 54.5 54.0 50.0 51.0 53.0 56.3 SEQ 82 63.569.8 69.9 53.7 53.9 66.4 66.6 SEQ 86 66.8 100 73.1 51.9 52.8 68.4 68.2SEQ 90 100 67.7 68.0 52.0 52.1 64.3 64.9 SEQ 94 67.7 100 72.8 51.9 52.868.2 68.2 SEQ 98 68.0 72.8 100 54.2 53.5 67.7 67.9 SEQ 52.0 51.9 54.2100 84.7 52.2 52.2 102 SEQ 52.1 52.8 53.5 84.7 100 53.5 53.5 130 SEQ64.3 68.2 67.7 52.2 53.5 100 100 134 SEQ 64.9 68.2 67.9 52.2 53.5 100100 138

Identity Matrix of Xanthan Lyase Sequences

SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ IDNO: 4 NO: 46 NO: 60 NO: 64 NO: 106 NO: 110 NO: 114 NO: 118 NO: 122 NO:126 SEQ ID NO: 4 100 100 50.8 66.1 52.1 53.3 50.3 53 55.8 66.2 SEQ IDNO: 46 100 100 48.4 62.0 49.4 50.8 47.9 50.3 49.1 64.9 SEQ ID NO: 6050.8 48.4 100 51.7 64.5 68.9 63.6 68.9 46.8 46.5 SEQ ID NO: 64 66.1 62.051.7 100 52.9 52.1 51.8 53.5 52.2 81.1 SEQ ID NO: 106 52.1 49.4 64.552.9 100 64.3 60.6 63.8 47.6 48.0 SEQ ID NO: 110 53.3 50.8 68.9 52.164.3 100 64.2 67.3 47.2 49.5 SEQ ID NO: 114 50.3 47.9 63.6 51.8 60.664.2 100 65.4 45.6 48.6 SEQ ID NO: 118 53 50.3 68.9 53.5 63.8 67.3 65.4100 48.0 49.6 SEQ ID NO: 122 55.8 49.1 46.8 52.2 47.6 47.2 45.6 48.0 10055.9 SEQ ID NO: 126 66.2 64.9 46.5 81.1 48.0 49.5 48.6 49.6 55.9 100

SHORT DESCRIPTION OF THE FIGURE

FIG. 1 shows a plasmid map of the linear vector with gene insert for SEQID NO: 87.

DEFINITIONS

Allelic variant: The term “allelic variant” means any of two or morealternative forms of a gene occupying the same chromosomal locus.Allelic variation arises naturally through mutation, and may result inpolymorphism within populations. Gene mutations can be silent (no changein the encoded polypeptide) or may encode polypeptides having alteredamino acid sequences. An allelic variant of a polypeptide is apolypeptide encoded by an allelic variant of a gene.

Catalytic domain: The term “catalytic domain” means the region of anenzyme containing the catalytic machinery of the enzyme.

cDNA: The term “cDNA” means a DNA molecule that can be prepared byreverse transcription from a mature, spliced, mRNA molecule obtainedfrom a eukaryotic or prokaryotic cell. cDNA lacks intron sequences thatmay be present in the corresponding genomic DNA. The initial, primaryRNA transcript is a precursor to mRNA that is processed through a seriesof steps, including splicing, before appearing as mature spliced mRNA.

Cleaning or Detergent Application: the term “cleaning or detergentapplication” means applying the endoglucanase of the application in anycomposition for the purpose of cleaning or washing, by hand, machine orautomated, a hard surface or a textile.

Cleaning or Detergent Composition: the term “cleaning or detergentcomposition” refers to compositions that find use in the removal ofundesired compounds from items to be cleaned, such as textiles, dishes,and hard surfaces. The terms encompass any materials/compounds selectedfor the particular type of cleaning composition desired and the form ofthe product (e.g., liquid, gel, powder, granulate, paste, or spraycompositions) and includes, but is not limited to, detergentcompositions (e.g., liquid and/or solid laundry detergents and finefabric detergents; hard surface cleaning formulations, such as forglass, wood, ceramic and metal counter tops and windows; carpetcleaners; oven cleaners; fabric fresheners; fabric softeners; andtextile and laundry pre-spotters, as well as dish wash detergents). Inaddition to the endoglucanase, the detergent formulation may contain oneor more additional enzymes (such as proteases, amylases, lipases,cutinases, cellulases, endoglucanases, xyloglucanases, pectinases,pectin lyases, xanthanases, peroxidaes, haloperoxygenases, catalases andmannanases, or any mixture thereof), and/or components such assurfactants, builders, chelators or chelating agents, bleach system orbleach components, polymers, fabric conditioners, foam boosters, sudssuppressors, dyes, perfume, tannish inhibitors, optical brighteners,bactericides, fungicides, soil suspending agents, anti corrosion agents,enzyme inhibitors or stabilizers, enzyme activators, transferase(s),hydrolytic enzymes, oxido reductases, bluing agents and fluorescentdyes, antioxidants, and solubilizers.

Coding sequence: The term “coding sequence” means a polynucleotide,which directly specifies the amino acid sequence of a polypeptide. Theboundaries of the coding sequence are generally determined by an openreading frame, which begins with a start codon such as ATG, GTG, or TTGand ends with a stop codon such as TAA, TAG, or TGA. The coding sequencemay be a genomic DNA, cDNA, synthetic DNA, or a combination thereof.

Colour clarification: During washing and wearing loose or broken fiberscan accumulate on the surface of the fabrics. One consequence can bethat the colours of the fabric appear less bright or less intensebecause of the surface contaminations. Removal of the loose or brokenfibers from the textile will partly restore the original colours andlooks of the textile. By the term “colour clarification”, as usedherein, is meant the partial restoration of the initial colours oftextile.

Control sequences: The term “control sequences” means nucleic acidsequences necessary for expression of a polynucleotide encoding a maturepolypeptide of the present invention. Each control sequence may benative (i.e., from the same gene) or foreign (i.e., from a differentgene) to the polynucleotide encoding the polypeptide or native orforeign to each other. Such control sequences include, but are notlimited to, a leader, polyadenylation sequence, propeptide sequence,promoter, signal peptide sequence, and transcription terminator. At aminimum, the control sequences include a promoter, and transcriptionaland translational stop signals. The control sequences may be providedwith linkers for the purpose of introducing specific restriction sitesfacilitating ligation of the control sequences with the coding region ofthe polynucleotide encoding a polypeptide.

Degrading xanthan gum: The term “degrading xanthan gum” is definedherein as the depolymerization, degradation or breaking down of xanthangum into smaller components. The degradation of xanthan gum can eitherbe the removal of one or more side chain saccharides, the cutting of thebackbone of xanthan gum into smaller components or the removal of one ormore side chain saccharides and the cutting of the backbone of xanthangum into smaller components. The degradation of xanthan gum canpreferably be measured using the viscosity reduction method as describedin example 6. Alternatively, the degradation of xanthan gum can bemeasured using the reducing ends method as described in example 6 or thecolourmetric assay as described in examples 25 and 26.

Delta remission value (ΔRem): The terms “Delta remission” or “Deltaremission value” are defined herein as the result of a reflectance orremission measurement at 460 nm. The swatch is measured with one swatchof similar colour as background, preferably a swatch from a repetitionwash. A swatch representing each swatch type is measured before wash.The Delta remission is the remission value of the washed swatch minusthe remission value of the unwashed swatch.

Delta enzyme performance value (ΔRem enzyme value): The term “Deltaenzyme remission value” is defined herein as the result of a reflectanceor remission measurement at 460 nm. The swatch is measured with oneswatch of similar colour as background, preferably a swatch from arepetition wash. A swatch representing each swatch type is measuredbefore wash. The Delta remission is the remission value of the swatchwashed in detergent with an enzyme present minus the remission value ofa similar swatch washed in a detergent without enzyme present.

Delta enzyme intensity value (ΔInt enzyme value): The terms “Deltaenzyme intensity” or “Delta enzyme intensity value” are defined hereinas the result of an enzyme intensity value as defined in AMSA assay. TheDelta intensity is the intensity value of the swatch area washed indetergent with an enzyme present minus the intensity value of the swatcharea washed in detergent without enzyme present

Detergent component: the term “detergent component” is defined herein tomean the types of chemicals which can be used in detergent compositions.Examples of detergent components are surfactants, hydrotropes, builders,co-builders, chelators or chelating agents, bleaching system or bleachcomponents, polymers, fabric hueing agents, fabric conditioners, foamboosters, suds suppressors, dispersants, dye transfer inhibitors,fluorescent whitening agents, perfume, optical brighteners,bactericides, fungicides, soil suspending agents, soil release polymers,anti-redeposition agents, enzyme inhibitors or stabilizers, enzymeactivators, antioxidants, and solubilizers. The detergent compositionmay comprise of one or more of any type of detergent component.

Detergent Composition: the term “detergent composition” refers tocompositions that find use in the removal of undesired compounds fromitems to be cleaned, such as textiles, dishes, and hard surfaces. Thedetergent composition may be used to e.g. clean textiles, dishes andhard surfaces for both household cleaning and industrial cleaning. Theterms encompass any materials/compounds selected for the particular typeof cleaning composition desired and the form of the product (e.g.,liquid, gel, powder, granulate, paste, or spray compositions) andincludes, but is not limited to, detergent compositions (e.g., liquidand/or solid laundry detergents and fine fabric detergents; hard surfacecleaning formulations, such as for glass, wood, ceramic and metalcounter tops and windows; carpet cleaners; oven cleaners; fabricfresheners; fabric softeners; and textile and laundry pre-spotters, aswell as dish wash detergents). In addition to containing a GH9endoglucanase of the invention and/or xanthan lyase of the invention,the detergent formulation may contain one or more additional enzymes(such as proteases, amylases, lipases, cutinases, cellulases,endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases,peroxidaes, haloperoxygenases, catalases and mannanases, or any mixturethereof), and/or components such as surfactants, builders, chelators orchelating agents, bleach system or bleach components, polymers, fabricconditioners, foam boosters, suds suppressors, dyes, perfume, tannishinhibitors, optical brighteners, bactericides, fungicides, soilsuspending agents, anti corrosion agents, enzyme inhibitors orstabilizers, enzyme activators, transferase(s), hydrolytic enzymes,oxido reductases, bluing agents and fluorescent dyes, antioxidants, andsolubilizers.

Dish wash: The term “dish wash” refers to all forms of washing dishes,e.g. by hand or automatic dish wash. Washing dishes includes, but is notlimited to, the cleaning of all forms of crockery such as plates, cups,glasses, bowls, all forms of cutlery such as spoons, knives, forks andserving utensils as well as ceramics, plastics, metals, china, glass andacrylics.

Dish washing composition: The term “dish washing composition” refers toall forms of compositions for cleaning hard surfaces. The presentinvention is not restricted to any particular type of dish washcomposition or any particular detergent.

Endoglucanase: The term “endoglucanase” means anendo-1,4-(1,3;1,4)-beta-D-glucan 4-glucanohydrolase (E.C. 3.2.1.4) thatcatalyzes endohydrolysis of 1,4-beta-D-glycosidic linkages in cellulose,cellulose derivatives (such as carboxymethyl cellulose and hydroxyethylcellulose), lichenin, beta-1,4 bonds in mixed beta-1,3 glucans such ascereal beta-D-glucans, xyloglucans, xanthans and other plant materialcontaining cellulosic components. Endoglucanase activity can bedetermined by measuring reduction in substrate viscosity or increase inreducing ends determined by a reducing sugar assay (Zhang et al., 2006,Biotechnology Advances 24: 452-481). For purposes of the presentinvention, endoglucanase activity is determined using carboxymethylcellulose (CMC) as substrate according to the procedure of Ghose, 1987,Pure and Appl. Chem. 59: 257-268, at pH 5, 40° C.

Enzyme Detergency benefit: The term “enzyme detergency benefit” isdefined herein as the advantageous effect an enzyme may add to adetergent compared to the same detergent without the enzyme. Importantdetergency benefits which can be provided by enzymes are stain removalwith no or very little visible soils after washing and or cleaning,prevention or reduction of redeposition of soils released in the washingprocess an effect that also is termed anti-redeposition, restoring fullyor partly the whiteness of textiles, which originally were white butafter repeated use and wash have obtained a greyish or yellowishappearance an effect that also is termed whitening. Textile carebenefits, which are not directly related to catalytic stain removal orprevention of redeposition of soils are also important for enzymedetergency benefits. Examples of such textile care benefits areprevention or reduction of dye transfer from one fabric to anotherfabric or another part of the same fabric an effect that is also termeddye transfer inhibition or anti-backstaining, removal of protruding orbroken fibers from a fabric surface to decrease pilling tendencies orremove already existing pills or fuzz an effect that also is termedanti-pilling, improvement of the fabric-softness, colour clarificationof the fabric and removal of particulate soils which are trapped in thefibers of the fabric or garment. Enzymatic bleaching is a further enzymedetergency benefit where the catalytic activity generally is used tocatalyze the formation of bleaching component such as hydrogen peroxideor other peroxides.

Expression: The term “expression” includes any step involved in theproduction of a polypeptide including, but not limited to,transcription, post-transcriptional modification, translation,post-translational modification, and secretion.

Expression vector: The term “expression vector” means a linear orcircular DNA molecule that comprises a polynucleotide encoding apolypeptide and is operably linked to control sequences that provide forits expression.

Fragment: The term “fragment” means a polypeptide or a catalytic domainhaving one or more (e.g., several) amino acids absent from the aminoand/or carboxyl terminus of a mature polypeptide or domain; wherein thefragment has xanthan degrading activity such as activity on xanthan gumpretreated with xanthan lyase or xanthan lyase activity

GH9 endoglucanases having activity on xanthan gum pretreated withxanthan lyase: The term “GH9 endoglucanases having activity on xanthangum pretreated with xanthan lyase” or an “endoglucanases having activityon xanthan gum pretreated with xanthan lyase and belonging to the GH9class of glycosyl hydrioases” is defined as a polypeptide comprising adomain belonging to the GH9 class of glycosyl hydrolases, and havingsignificant activity on xanthan gum pretreated with xanthan lyase. Inone aspect of the invention a GH9 endoglucanases having activity onxanthan gum pretreated with xanthan lyase may be a polypeptide having asequence selected among SEQ ID NO: 2, SEQ ID NO: 10, SEQ ID NO: 12, SEQID NO: 14, SEQ ID NO: 48, SEQ ID NO: 52, SEQ ID NO: 56, SEQ ID NO: 82,SEQ ID NO: 86, SEQ ID NO: 90, SEQ ID NO: 94, SEQ ID NO: 98, SEQ ID NO:102, SEQ ID NO: 130, SEQ ID NO: 134 and SEQ ID NO: 138. In a particularthe GH9 endoglucanase having activity on xanthan gum pretreated withxanthan lyase has higher specificity of xanthan gum pretreated withxanthan lyase the specific activity on CMC (carboxymethylcellulose)which is known as an excellent substrate for endoglucanases. Activity onxanthan gum pretreated with xanthan lyase can be determined as disclosedin Example 8 below.

Hard surface cleaning: The term “Hard surface cleaning” is definedherein as cleaning of hard surfaces wherein hard surfaces may includefloors, tables, walls, roofs etc. as well as surfaces of hard objectssuch as cars (car wash) and dishes (dish wash). Dish washing includesbut are not limited to cleaning of plates, cups, glasses, bowls, andcutlery such as spoons, knives, forks, serving utensils, ceramics,plastics, metals, china, glass and acrylics.

Host cell: The term “host cell” means any cell type that is susceptibleto transformation, transfection, transduction, or the like with anucleic acid construct or expression vector comprising a polynucleotideof the present invention. The term “host cell” encompasses any progenyof a parent cell that is not identical to the parent cell due tomutations that occur during replication.

Improved wash performance: The term “improved wash performance” isdefined herein as a (variant) enzyme (also a blend of enzymes, notnecessarily only variants but also backbones, and in combination withcertain cleaning composition etc.) displaying an alteration of the washperformance of a protease variant relative to the wash performance ofthe parent protease variant e.g. by increased stain removal. The term“wash performance” includes wash performance in laundry but also e.g. indish wash.

Isolated: The term “isolated” means a substance in a form or environmentthat does not occur in nature. Non-limiting examples of isolatedsubstances include (1) any non-naturally occurring substance, (2) anysubstance including, but not limited to, any enzyme, variant, nucleicacid, protein, peptide or cofactor, that is at least partially removedfrom one or more or all of the naturally occurring constituents withwhich it is associated in nature; (3) any substance modified by the handof man relative to that substance found in nature; or (4) any substancemodified by increasing the amount of the substance relative to othercomponents with which it is naturally associated (e.g., multiple copiesof a gene encoding the substance; use of a stronger promoter than thepromoter naturally associated with the gene encoding the substance). Anisolated substance may be present in a fermentation broth sample.

Laundering: The term “laundering” relates to both household launderingand industrial laundering and means the process of treating textileswith a solution containing a cleaning or detergent composition of thepresent invention. The laundering process can for example be carried outusing e.g. a household or an industrial washing machine or can becarried out by hand.

Mature polypeptide: The term “mature polypeptide” means a polypeptide inits final form following translation and any post-translationalmodifications, such as N-terminal processing, C-terminal truncation,glycosylation, phosphorylation, etc. In one aspect, the maturepolypeptide is amino acids 1 to 1055 of SEQ ID NO: 2 based on theSignalP program (Nielsen et al., 1997, Protein Engineering 10: 1-6) thatpredicts amino acids −38 to −1 of SEQ ID NO: 2 are a signal peptide. Inanother aspect, the mature polypeptide is amino acids 1 to 918 of SEQ IDNO: 10 based on the SignalP program that predicts amino acids −33 to −1of SEQ ID NO: 10 are a signal peptide. In a further aspect, the maturepolypeptide is amino acids 1 to 916 of SEQ ID NO: 12 based on theSignalP program that predicts amino acids −32 to −1 of SEQ ID NO: 12 area signal peptide. In one aspect, the mature polypeptide is amino acids 1to 918 of SEQ ID NO: 14 based on the SignalP program that predicts aminoacids −33 to −1 of SEQ ID NO: 14 are a signal peptide. In anotheraspect, the mature polypeptide is amino acids 1 to 1007 of SEQ ID NO: 48based on the SignalP program that predicts amino acids −36 to −1 of SEQID NO: 48 are a signal peptide. In a further aspect, the maturepolypeptide is amino acids 1 to 915 of SEQ ID NO: 52 based on theSignalP program that predicts amino acids −36 to −1 of SEQ ID NO: 52 area signal peptide. In an additional aspect, the mature polypeptide isamino acids 1 to 1056 of SEQ ID NO: 56 based on the SignalP program thatpredicts amino acids −38 to −1 of SEQ ID NO: 56 are a signal peptide.

In one aspect, the mature polypeptide is amino acids 1 to 1371 of SEQ IDNO: 82 based on the SignalP program that predicts amino acids −37 to −1of SEQ ID NO: 82 are a signal peptide. In another aspect, the maturepolypeptide is amino acids 1 to 1203 of SEQ ID NO: 86 based on theSignalP program that predicts amino acids −37 to −1 of SEQ ID NO: 86 area signal peptide. In a further aspect, the mature polypeptide is aminoacids 1 to 1379 of SEQ ID NO: 90 based on the SignalP program thatpredicts amino acids −37 to −1 of SEQ ID NO: 90 are a signal peptide. Inan additional aspect, the mature polypeptide is amino acids 1 to 1371 ofSEQ ID NO: 94 based on the SignalP program that predicts amino acids −37to −1 of SEQ ID NO: 94 are a signal peptide. In one aspect, the maturepolypeptide is amino acids 1 to 1372 of SEQ ID NO: 98 based on theSignalP program that predicts amino acids −37 to −1 of SEQ ID NO: 98 area signal peptide. In another aspect, the mature polypeptide is aminoacids 1 to 922 of SEQ ID NO: 102 based on the SignalP program thatpredicts amino acids −32 to −1 of SEQ ID NO: 102 are a signal peptide.In a further aspect, the mature polypeptide is amino acids 1 to 916 ofSEQ ID NO: 130 based on the SignalP program that predicts amino acids−36 to −1 of SEQ ID NO: 130 are a signal peptide. In an additionalaspect, the mature polypeptide is amino acids 1 to 1373 of SEQ ID NO:134 based on the SignalP program that predicts amino acids −37 to −1 ofSEQ ID NO: 134 are a signal peptide. In an additional aspect, the maturepolypeptide is amino acids 1 to 1204 of SEQ ID NO: 138 based on theSignalP program that predicts amino acids −37 to −1 of SEQ ID NO: 138are a signal peptide.

In one aspect, the mature polypeptide is amino acids 1 to 760 of SEQ IDNO: 4 based on the SignalP program that predicts amino acids −31 to −1of SEQ ID NO: 4 are a signal peptide. In another aspect, the maturepolypeptide is amino acids 1 to 1043 of SEQ ID NO: 46 based on theSignalP program that predicts amino acids −31 to −1 of SEQ ID NO: 46 area signal peptide. In a further aspect, the mature polypeptide is aminoacids 1 to 896 of SEQ ID NO: 60 based on the SignalP program thatpredicts amino acids −41 to −1 of SEQ ID NO: 60 are a signal peptide. Inone aspect, the mature polypeptide is amino acids 1 to 1038 of SEQ IDNO: 64 based on the SignalP program that predicts amino acids −24 to −1of SEQ ID NO: 64 are a signal peptide.

In one aspect, the mature polypeptide is amino acids 1 to 901 of SEQ IDNO: 106 based on the SignalP program that predicts amino acids −32 to −1of SEQ ID NO: 106 are a signal peptide. In another aspect, the maturepolypeptide is amino acids 1 to 899 of SEQ ID NO: 110 based on theSignalP program that predicts amino acids −32 to −1 of SEQ ID NO: 110are a signal peptide. In a further aspect, the mature polypeptide isamino acids 1 to 897 of SEQ ID NO: 114 based on the SignalP program thatpredicts amino acids −61 to −1 of SEQ ID NO: 114 are a signal peptide.In an additional aspect, the mature polypeptide is amino acids 1 to 933of SEQ ID NO: 118 based on the SignalP program that predicts amino acids−27 to −1 of SEQ ID NO: 118 are a signal peptide. In one aspect, themature polypeptide is amino acids 1 to 1049 of SEQ ID NO: 122 based onthe SignalP program that predicts amino acids −42 to −1 of SEQ ID NO:122 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 900 of SEQ ID NO: 126 based on the SignalP program thatpredicts amino acids −33 to −1 of SEQ ID NO: 126 are a signal peptide.

It is known in the art that a host cell may produce a mixture of two ofmore different mature polypeptides (i.e., with a different C-terminaland/or N-terminal amino acid) expressed by the same polynucleotide. Itis also known in the art that different host cells process polypeptidesdifferently, and thus, one host cell expressing a polynucleotide mayproduce a different mature polypeptide (e.g., having a differentC-terminal and/or N-terminal amino acid) as compared to another hostcell expressing the same polynucleotide.

Mature polypeptide coding sequence: The term “mature polypeptide codingsequence” means a polynucleotide that encodes a mature polypeptidehaving enzymatic activity such as activity on xanthan gum pretreatedwith xanthan lyase or xanthan lyase activity. In one aspect, the maturepolypeptide coding sequence is nucleotides 115 to 3279 of SEQ ID NO: 1based on the SignalP program (Nielsen et al., 1997, supra) that predictsnucleotides 1 to 114 of SEQ ID NO: 1 encode a signal peptide. In anotheraspect, the mature polypeptide coding sequence is nucleotides 94 to 2373of SEQ ID NO: 3 based on the SignalP program that predicts nucleotides 1to 93 of SEQ ID NO: 3 encode a signal peptide. In a further aspect, themature polypeptide coding sequence is nucleotides 600 to 3353 of SEQ IDNO: 9 based on the SignalP program that predicts nucleotides 501 to 599of SEQ ID NO: 9 encode a signal peptide. In one aspect, the maturepolypeptide coding sequence is nucleotides 174 to 2921 of SEQ ID NO: 11based on the SignalP program that predicts nucleotides 78 to 173 of SEQID NO: 11 encode a signal peptide. In another aspect, the maturepolypeptide coding sequence is nucleotides 200 to 2953 of SEQ ID NO: 13based on the SignalP program that predicts nucleotides 101 to 199 of SEQID NO: 13 encode a signal peptide. In a further aspect, the maturepolypeptide coding sequence is nucleotides 209 to 3337 of SEQ ID NO: 45based on the SignalP program that predicts nucleotides 116 to 208 of SEQID NO: 45 encode a signal peptide. In one aspect, the mature polypeptidecoding sequence is nucleotides 109 to 3129 of SEQ ID NO: 47 based on theSignalP program that predicts nucleotides 1 to 108 of SEQ ID NO: 47encode a signal peptide. In another aspect, the mature polypeptidecoding sequence is nucleotides 109 to 2853 of SEQ ID NO: 51 based on theSignalP program that predicts nucleotides 1 to 108 of SEQ ID NO: 51encode a signal peptide. In a further aspect, the mature polypeptidecoding sequence is nucleotides 115 to 3282 of SEQ ID NO: 55 based on theSignalP program that predicts nucleotides 1 to 114 of SEQ ID NO: 55encode a signal peptide. In an additional aspect, the mature polypeptidecoding sequence is nucleotides 124 to 2811 of SEQ ID NO: 59 based on theSignalP program that predicts nucleotides 1 to 123 of SEQ ID NO: 59encode a signal peptide. In one aspect, the mature polypeptide codingsequence is nucleotides 73 to 3195 of SEQ ID NO: 63 based on the SignalPprogram that predicts nucleotides 1 to 72 of SEQ ID NO: 63 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 112to 4224 of SEQ ID NO: 81 based on the SignalP program that predictsnucleotides 1 to 111 of SEQ ID NO: 81 encode a signal peptide. Inanother aspect, the mature polypeptide coding sequence is nucleotides112 to 3720 of SEQ ID NO: 85 based on the SignalP program that predictsnucleotides 1 to 111 of SEQ ID NO: 85 encode a signal peptide. In afurther aspect, the mature polypeptide coding sequence is nucleotides112 to 4248 of SEQ ID NO: 89 based on the SignalP program that predictsnucleotides 1 to 111 of SEQ ID NO: 89 encode a signal peptide. In anadditional aspect, the mature polypeptide coding sequence is nucleotides112 to 4224 of SEQ ID NO: 93 based on the SignalP program that predictsnucleotides 1 to 111 of SEQ ID NO: 93 encode a signal peptide. In oneaspect, the mature polypeptide coding sequence is nucleotides 112 to4227 of SEQ ID NO: 97 based on the SignalP program that predictsnucleotides 1 to 111 of SEQ ID NO: 97 encode a signal peptide. Inanother aspect, the mature polypeptide coding sequence is nucleotides 76to 2841 of SEQ ID NO: 101 based on the SignalP program that predictsnucleotides 1 to 75 of SEQ ID NO: 101 encode a signal peptide. In afurther aspect, the mature polypeptide coding sequence is nucleotides 97to 2799 of SEQ ID NO: 105 based on the SignalP program that predictsnucleotides 1 to 96 of SEQ ID NO: 105 encode a signal peptide. In anadditional aspect, the mature polypeptide coding sequence is nucleotides97 to 2793 of SEQ ID NO: 109 based on the SignalP program that predictsnucleotides 1 to 96 of SEQ ID NO: 109 encode a signal peptide. In oneaspect, the mature polypeptide coding sequence is nucleotides 184 to2874 of SEQ ID NO: 113 based on the SignalP program that predictsnucleotides 1 to 183 of SEQ ID NO: 113 encode a signal peptide. Inanother aspect, the mature polypeptide coding sequence is nucleotides 82to 2880 of SEQ ID NO: 117 based on the SignalP program that predictsnucleotides 1 to 81 of SEQ ID NO: 117 encode a signal peptide. In afurther aspect, the mature polypeptide coding sequence is nucleotides127 to 3273 of SEQ ID NO: 121 based on the SignalP program that predictsnucleotides 1 to 126 of SEQ ID NO: 121 encode a signal peptide. In anadditional aspect, the mature polypeptide coding sequence is nucleotides100 to 2799 of SEQ ID NO: 125 based on the SignalP program that predictsnucleotides 1 to 99 of SEQ ID NO: 125 encode a signal peptide. In oneaspect, the mature polypeptide coding sequence is nucleotides 97 to 2844of SEQ ID NO: 129 based on the SignalP program that predicts nucleotides1 to 96 of SEQ ID NO: 129 encode a signal peptide. In another aspect,the mature polypeptide coding sequence is nucleotides 112 to 4230 of SEQID NO: 133 based on the SignalP program that predicts nucleotides 1 to111 of SEQ ID NO: 133 encode a signal peptide. In a further aspect, themature polypeptide coding sequence is nucleotides 112 to 3723 of SEQ IDNO: 137 based on the SignalP program that predicts nucleotides 1 to 111of SEQ ID NO: 137 encode a signal peptide.

Nucleic acid construct: The term “nucleic acid construct” means anucleic acid molecule, either single- or double-stranded, which isisolated from a naturally occurring gene or is modified to containsegments of nucleic acids in a manner that would not otherwise exist innature or which is synthetic, which comprises one or more controlsequences.

Operably linked: The term “operably linked” means a configuration inwhich a control sequence is placed at an appropriate position relativeto the coding sequence of a polynucleotide such that the controlsequence directs expression of the coding sequence.

Sequence identity: The relatedness between two amino acid sequences orbetween two nucleotide sequences is described by the parameter “sequenceidentity”. For purposes of the present invention, the sequence identitybetween two amino acid sequences is determined using theNeedleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol.48: 443-453) as implemented in the Needle program of the EMBOSS package(EMBOSS: The European Molecular Biology Open Software Suite, Rice etal., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 orlater. The parameters used are gap open penalty of 10, gap extensionpenalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62)substitution matrix. The output of Needle labeled “longest identity”(obtained using the -nobrief option) is used as the percent identity andis calculated as follows:(Identical Residues×100)/(Length of Alignment−Total Number of Gaps inAlignment)

For purposes of the present invention, the sequence identity between twodeoxyribonucleotide sequences is determined using the Needleman-Wunschalgorithm (Needleman and Wunsch, 1970, supra) as implemented in theNeedle program of the EMBOSS package (EMBOSS: The European MolecularBiology Open Software Suite, Rice et al., 2000, supra), preferablyversion 5.0.0 or later. The parameters used are gap open penalty of 10,gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBINUC4.4) substitution matrix. The output of Needle labeled “longestidentity” (obtained using the -nobrief option) is used as the percentidentity and is calculated as follows:(Identical Deoxyribonucleotides×100)/(Length of Alignment−Total Numberof Gaps in Alignment)

Stringency conditions: The different stringency conditions are definedas follows.

The term “very low stringency conditions” means for probes of at least100 nucleotides in length, prehybridization and hybridization at 42° C.in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmonsperm DNA, and 25% formamide, following standard Southern blottingprocedures for 12 to 24 hours. The carrier material is finally washedthree times each for 15 minutes using 2×SSC, 0.2% SDS at 45° C.

The term “low stringency conditions” means for probes of at least 100nucleotides in length, prehybridization and hybridization at 42° C. in5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon spermDNA, and 25% formamide, following standard Southern blotting proceduresfor 12 to 24 hours. The carrier material is finally washed three timeseach for 15 minutes using 2×SSC, 0.2% SDS at 50° C.

The term “medium stringency conditions” means for probes of at least 100nucleotides in length, prehybridization and hybridization at 42° C. in5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon spermDNA, and 35% formamide, following standard Southern blotting proceduresfor 12 to 24 hours. The carrier material is finally washed three timeseach for 15 minutes using 2×SSC, 0.2% SDS at 55° C.

The term “medium-high stringency conditions” means for probes of atleast 100 nucleotides in length, prehybridization and hybridization at42° C. in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denaturedsalmon sperm DNA, and 35% formamide, following standard Southernblotting procedures for 12 to 24 hours. The carrier material is finallywashed three times each for 15 minutes using 2×SSC, 0.2% SDS at 60° C.

The term “high stringency conditions” means for probes of at least 100nucleotides in length, prehybridization and hybridization at 42° C. in5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon spermDNA, and 50% formamide, following standard Southern blotting proceduresfor 12 to 24 hours. The carrier material is finally washed three timeseach for 15 minutes using 2×SSC, 0.2% SDS at 65° C.

The term “very high stringency conditions” means for probes of at least100 nucleotides in length, prehybridization and hybridization at 42° C.in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmonsperm DNA, and 50% formamide, following standard Southern blottingprocedures for 12 to 24 hours. The carrier material is finally washedthree times each for 15 minutes using 2×SSC, 0.2% SDS at 70° C.

Subsequence: The term “subsequence” means a polynucleotide having one ormore (e.g., several) nucleotides absent from the 5′ and/or 3′ end of amature polypeptide coding sequence; wherein the subsequence encodes afragment having enzymatic activity, such as activity on xanthan gumpretreated with xanthan lyase or xanthan lyase activity.

Textile: The term “textile” means any textile material including yarns,yarn intermediates, fibers, non-woven materials, natural materials,synthetic materials, and any other textile material, fabrics made ofthese materials and products made from fabrics (e.g., garments and otherarticles). The textile or fabric may be in the form of knits, wovens,denims, non-wovens, felts, yarns, and toweling. The textile may becellulose based such as natural cellulosics, including cotton,flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g.originating from wood pulp) including viscose/rayon, ramie, celluloseacetate fibers (tricell), lyocell or blends thereof. The textile orfabric may also be non-cellulose based such as natural polyamidesincluding wool, camel, cashmere, mohair, rabbit and silk or syntheticpolymer such as nylon, aramid, polyester, acrylic, polypropylene andspandex/elastane, or blends thereof as well as blend of cellulose basedand non-cellulose based fibers. Examples of blends are blends of cottonand/or rayon/viscose with one or more companion material such as wool,synthetic fibers (e.g. polyamide fibers, acrylic fibers, polyesterfibers, polyvinyl alcohol fibers, polyvinyl chloride fibers,polyurethane fibers, polyurea fibers, aramid fibers), andcellulose-containing fibers (e.g. rayon/viscose, ramie, flax/linen,jute, cellulose acetate fibers, lyocell). Fabric may be conventionalwashable laundry, for example stained household laundry. When the termfabric or garment is used it is intended to include the broader termtextiles as well.

Textile care benefit: “Textile care benefits”, which are not directlyrelated to catalytic stain removal or prevention of redeposition ofsoils, are also important for enzyme detergency benefits. Examples ofsuch textile care benefits are prevention or reduction of dye transferfrom one textile to another textile or another part of the same textilean effect that is also termed dye transfer inhibition oranti-backstaining, removal of protruding or broken fibers from a textilesurface to decrease pilling tendencies or remove already existing pillsor fuzz an effect that also is termed anti-pilling, improvement of thetextile-softness, colour clarification of the textile and removal ofparticulate soils which are trapped in the fibers of the textile.Enzymatic bleaching is a further enzyme detergency benefit where thecatalytic activity generally is used to catalyze the formation ofbleaching component such as hydrogen peroxide or other peroxides orother bleaching species.

Variant: The term “variant” means an GH9 endoglucanase having activityon xanthan gum pretreated with xanthan lyase e., a substitution,insertion, and/or deletion, at one or more (e.g., several) positions. Asubstitution means replacement of the amino acid occupying a positionwith a different amino acid; a deletion means removal of the amino acidoccupying a position; and an insertion means adding one or more (e.g.several) amino acids e.g. 1-5 amino acids adjacent to and immediatelyfollowing the amino acid occupying a position.

In one embodiment the term “variant” means a polypeptide having xanthanlyase activity comprising an alteration, i.e., a substitution,insertion, and/or deletion, at one or more (e.g., several) positions. Asubstitution means replacement of the amino acid occupying a positionwith a different amino acid; a deletion means removal of the amino acidoccupying a position; and an insertion means adding one or more (e.g.several) amino acids e.g. 1-5 amino acids adjacent to and immediatelyfollowing the amino acid occupying a position.

In another embodiment the term “variant” means a GH9 endoglucanaseshaving activity on xanthan gum pretreated with xanthan lyase comprisingan alteration, i.e., a substitution, insertion, and/or deletion, at oneor more (e.g., several) positions. A substitution means replacement ofthe amino acid occupying a position with a different amino acid; adeletion means removal of the amino acid occupying a position; and aninsertion means adding one or more (e.g. several) amino acids e.g. 1-5amino acids adjacent to and immediately following the amino acidoccupying a position.

Wash performance: The term “wash performance” is used as an enzyme'sability to remove stains present on the object to be cleaned during e.g.wash or hard surface cleaning. The improvement in the wash performancemay be quantified by calculating the so-called intensity value (Int) asdefined in ‘Automatic Mechanical Stress Assay (AMSA) for laundry’ hereinor the remission value (Rem) as defined herein. See also the washperformance test in Examples 9, 18, 19, 28, 31 and 32 herein.

Whiteness: The term “Whiteness” is defined herein as a broad term withdifferent meanings in different regions and for different customers.Loss of whiteness can e.g. be due to greying, yellowing, or removal ofoptical brighteners/hueing agents. Greying and yellowing can be due tosoil redeposition, body soils, colouring from e.g. iron and copper ionsor dye transfer. Whiteness might include one or several issues from thelist below: Colorant or dye effects; Incomplete stain removal (e.g. bodysoils, sebum etc.); Re-deposition (greying, yellowing or otherdiscolorations of the object) (removed soils re-associates with otherpart of textile, soiled or unsoiled); Chemical changes in textile duringapplication; and Clarification or brightening of colours.

Xanthan Lyase: The term “xanthan lyase” is defined herein as an enzymethat cleaves the β-D-mannosyl-β-D-1,4-glucuronosyl bonds in xanthan gum(EC 4.2.2.12). For purposes of the present invention, xanthan lyaseactivity is determined according to the procedure described in theExamples. In one aspect, the polypeptides of the present invention haveat least 20%, e.g., at least 40%, at least 50%, at least 60%, at least70%, at least 80%, at least 90%, at least 95%, or at least 100% of thexanthan lyase activity of the mature polypeptide of SEQ ID NO: 4, SEQ IDNO: 46, SEQ ID NO: 60 or SEQ ID NO: 64. Xanthan lyase activity may bedetermined as described in the ‘Xanthan lyase activity assay’ asdescribed in the Example section.

DETAILED DESCRIPTION OF THE INVENTION

The present invention provides polypeptides having xanthan lyaseactivity and to GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and polynucleotides encoding thepolypeptides. The GH9 endoglucanase class of enzymes has not previouslybeen shown to degrade xanthan. In addition, the combination of xanthanlyase and an GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase of the invention shows a synergisticimproved wash performance over using xanthan lyase or GH9 endoglucanaseshaving activity on xanthan gum pretreated with xanthan lyase alone.

GH9 Endoglucanases Having Activity on Xanthan Gum Pretreated withXanthan Lyase and Polypeptides Having Xanthan Lyase Activity

In an embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 2 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%, which have xanthan degrading activity.

In an embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 2 of at least 80%, e.g., at least 85%, at least 90%, at least 91%,at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 2. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 2.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 2 or an allelic variantthereof; or is a fragment thereof having endoglucanase activity andactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the polypeptide comprises or consists of the mature polypeptideof SEQ ID NO: 2. In another aspect, the polypeptide comprises orconsists of amino acids 1 to 1055 of SEQ ID NO: 2.

In another embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 10 of at least 85%, e.g., at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%, which have xanthan degrading activity.

In an embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 10 of at least 80%, e.g., at least 85%, at least 90%, at least 91%,at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 10. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 10.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 10 or an allelic variantthereof; or is a fragment thereof having endoglucanase activity andhaving activity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the polypeptide comprises or consists of the mature polypeptideof SEQ ID NO: 10. In another aspect, the polypeptide comprises orconsists of amino acids 1 to 918 of SEQ ID NO: 10.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 12 of at least 90%, e.g., at least 91%, at least 92%, at least 93%,at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 12. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 12.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 12 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 12. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 916 of SEQ ID NO: 12.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 14 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 14. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 14.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 14 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 14. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 918 of SEQ ID NO: 14.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 48 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 48. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 48.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 48 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 48. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1007 of SEQ ID NO: 48.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 52 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 52. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 52.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 52 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 52. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 915 of SEQ ID NO: 52.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 56 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 56. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 56.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 56 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 56. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1056 of SEQ ID NO: 56.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 82 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 82. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 82.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 82 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 82. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1371 of SEQ ID NO: 82.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 86 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 86. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 86.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 86 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 86. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1203 of SEQ ID NO: 86.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 90 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 90. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 90.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 90 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 90. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1379 of SEQ ID NO: 90.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 94 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 94. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 94.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 94 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 94. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1371 of SEQ ID NO: 94.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 98 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 98. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 98.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 98 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 98. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1372 of SEQ ID NO: 98.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 130 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 130. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 130.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 130 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 130. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 916 of SEQ ID NO: 130.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 134 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 134. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 134.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 134 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 134. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1373 of SEQ ID NO: 134.

In a further embodiment, the present invention relates to isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 138 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 138. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 138.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 138 or an allelic variantthereof; or is a fragment thereof having activity on xanthan gumpretreated with xanthan lyase. In another aspect, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 138. Inanother aspect, the polypeptide comprises or consists of amino acids 1to 1204 of SEQ ID NO: 138.

In another embodiment, the present invention relates to an isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide that hybridizes under mediumstringency conditions, medium-high stringency conditions, highstringency conditions, or very high stringency conditions with themature polypeptide coding sequence of SEQ ID NO: 1, SEQ ID NO: 47, SEQID NO: 51, SEQ ID NO: 55, SEQ ID NO: 81, SEQ ID NO: 85, SEQ ID NO: 89,SEQ ID NO: 93, SEQ ID NO: 97, SEQ ID NO: 129, SEQ ID NO: 133, SEQ ID NO:137, or the full-length complement thereof (Sambrook et al., 1989,Molecular Cloning, A Laboratory Manual, 2d edition, Cold Spring Harbor,N.Y.). In a further embodiment, the present invention relates to anisolated GH9 endoglucanases having activity on xanthan gum pretreatedwith xanthan lyase encoded by a polynucleotide that hybridizes underhigh stringency conditions, or very high stringency conditions with themature polypeptide coding sequence of SEQ ID NO: 9, SEQ ID NO: 11, SEQID NO: 13 or the full-length complement thereof.

The polynucleotide of SEQ ID NO: 1, SEQ ID NO: 9, SEQ ID NO: 11, SEQ IDNO: 13, SEQ ID NO: 47, SEQ ID NO: 51, SEQ ID NO: 55, SEQ ID NO: 81, SEQID NO: 85, SEQ ID NO: 89, SEQ ID NO: 93, SEQ ID NO: 97, SEQ ID NO: 129,SEQ ID NO: 133 or SEQ ID NO: 137, or a subsequence thereof, as well asthe polypeptide of SEQ ID NO: 2, SEQ ID NO: 10, SEQ ID NO: 12, SEQ IDNO: 14, SEQ ID NO: 48, SEQ ID NO: 52, SEQ ID NO: 56, SEQ ID NO: 82, SEQID NO: 86, SEQ ID NO: 90, SEQ ID NO: 94, SEQ ID NO: 98, SEQ ID NO: 130,SEQ ID NO: 134, SEQ ID NO: 138, or a fragment thereof, may be used todesign nucleic acid probes to identify and clone DNA encoding GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase from strains of different genera or species according to methodswell known in the art. In particular, such probes can be used forhybridization with the genomic DNA or cDNA of a cell of interest,following standard Southern blotting procedures, in order to identifyand isolate the corresponding gene therein. Such probes can beconsiderably shorter than the entire sequence, but should be at least15, e.g., at least 25, at least 35, or at least 70 nucleotides inlength. Preferably, the nucleic acid probe is at least 100 nucleotidesin length, e.g., at least 200 nucleotides, at least 300 nucleotides, atleast 400 nucleotides, at least 500 nucleotides, at least 600nucleotides, at least 700 nucleotides, at least 800 nucleotides, or atleast 900 nucleotides in length. Both DNA and RNA probes can be used.The probes are typically labelled for detecting the corresponding gene(for example, with ³²P, ³H, ³⁵S, biotin, or avidin). Such probes areencompassed by the present invention.

A genomic DNA or cDNA library prepared from such other strains may bescreened for DNA that hybridizes with the probes described above andencodes a GH9 endoglucanase having activity on xanthan gum pretreatedwith xanthan lyase. Genomic or other DNA from such other strains may beseparated by agarose or polyacrylamide gel electrophoresis, or otherseparation techniques. DNA from the libraries or the separated DNA maybe transferred to and immobilized on nitrocellulose or other suitablecarrier material. In order to identify a clone or DNA that hybridizeswith SEQ ID NO: 1, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ IDNO: 47, SEQ ID NO: 51, SEQ ID NO: 55, SEQ ID NO: 81, SEQ ID NO: 85, SEQID NO: 89, SEQ ID NO: 93, SEQ ID NO: 97, SEQ ID NO: 129, SEQ ID NO: 133or SEQ ID NO: 137, or a subsequence thereof, the carrier material isused in a Southern blot.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 4 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 4. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 4.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 4 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 4. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 760 of SEQ ID NO: 4.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 46 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 46. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 46.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 46 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 46. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 1043 of SEQ ID NO: 46.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 60 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 60. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 60.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 60 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 60. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 896 of SEQ ID NO: 60.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 64 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 64. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 64.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 64 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 64. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 1038 of SEQ ID NO: 64.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 106 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 106. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 106.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 106 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 106. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 901 of SEQ ID NO: 106.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 110 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 110. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 110.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 110 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 110. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 899 of SEQ ID NO: 110.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 114 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 114. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 114.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 114 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 114. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 897 of SEQ ID NO: 114.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 118 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 118. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 118.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 118 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 118. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 933 of SEQ ID NO: 118.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 122 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 122. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 122.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 122 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 122. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 1049 of SEQ ID NO: 122.

In an embodiment, the present invention relates to isolated polypeptideshaving xanthan lyase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 126 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 126. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 126.

A polypeptide of the present invention preferably comprises or consistsof the amino acid sequence of SEQ ID NO: 126 or an allelic variantthereof; or is a fragment thereof having xanthan lyase activity. Inanother aspect, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 126. In another aspect, the polypeptidecomprises or consists of amino acids 1 to 900 of SEQ ID NO: 126.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidethat hybridizes under medium stringency conditions, medium-highstringency conditions, high stringency conditions, or very highstringency conditions with the mature polypeptide coding sequence of SEQID NO: 3, SEQ ID NO: 45, SEQ ID NO: 59, SEQ ID NO: 63, SEQ ID NO: 105,SEQ ID NO: 109, SEQ ID NO: 113, SEQ ID NO: 117, SEQ ID NO: 121, SEQ IDNO: 125, or the full-length complement thereof (Sambrook et al., 1989,Molecular Cloning, A Laboratory Manual, 2d edition, Cold Spring Harbor,N.Y.).

The polynucleotide of SEQ ID NO: 3, SEQ ID NO: 45, SEQ ID NO: 59, SEQ IDNO: 63, SEQ ID NO: 105, SEQ ID NO: 109, SEQ ID NO: 113, SEQ ID NO: 117,SEQ ID NO: 121, SEQ ID NO: 125, or a subsequence thereof, as well as thepolypeptide of SEQ ID NO: 4, SEQ ID NO: 46, SEQ ID NO: 60, SEQ ID NO:64, SEQ ID NO: 106, SEQ ID NO: 110, SEQ ID NO: 114, SEQ ID NO: 118, SEQID NO: 122, SEQ ID NO: 126 or a fragment thereof, may be used to designnucleic acid probes to identify and clone DNA encoding polypeptideshaving xanthan lyase activity from strains of different genera orspecies according to methods well known in the art. In particular, suchprobes can be used for hybridization with the genomic DNA or cDNA of acell of interest, following standard Southern blotting procedures, inorder to identify and isolate the corresponding gene therein. Suchprobes can be considerably shorter than the entire sequence, but shouldbe at least 15, e.g., at least 25, at least 35, or at least 70nucleotides in length. Preferably, the nucleic acid probe is at least100 nucleotides in length, e.g., at least 200 nucleotides, at least 300nucleotides, at least 400 nucleotides, at least 500 nucleotides, atleast 600 nucleotides, at least 700 nucleotides, at least 800nucleotides, or at least 900 nucleotides in length. Both DNA and RNAprobes can be used. The probes are typically labelled for detecting thecorresponding gene (for example, with ³²P, ³H, ³⁵S, biotin, or avidin).Such probes are encompassed by the present invention.

A genomic DNA or cDNA library prepared from such other strains may bescreened for DNA that hybridizes with the probes described above andencodes a polypeptide having xanthan lyase activity. Genomic or otherDNA from such other strains may be separated by agarose orpolyacrylamide gel electrophoresis, or other separation techniques. DNAfrom the libraries or the separated DNA may be transferred to andimmobilized on nitrocellulose or other suitable carrier material. Inorder to identify a clone or DNA that hybridizes with SEQ ID NO: 3, SEQID NO: 45, SEQ ID NO: 59, SEQ ID NO: 63, SEQ ID NO: 105, SEQ ID NO: 109,SEQ ID NO: 113, SEQ ID NO: 117, SEQ ID NO: 121, SEQ ID NO: 125 or asubsequence thereof, the carrier material is used in a Southern blot.

For purposes of the present invention, hybridization indicates that thepolynucleotide hybridizes to a labelled nucleic acid probe correspondingto (i) SEQ ID NO: 1, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ IDNO: 47, SEQ ID NO: 51, SEQ ID NO: 55, SEQ ID NO: 81, SEQ ID NO: 85, SEQID NO: 89, SEQ ID NO: 93, SEQ ID NO: 97, SEQ ID NO: 129, SEQ ID NO: 133or SEQ ID NO: 137; (ii) the mature polypeptide coding sequence of SEQ IDNO: 1, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 47, SEQ IDNO: 51, SEQ ID NO: 55, SEQ ID NO: 81, SEQ ID NO: 85, SEQ ID NO: 89, SEQID NO: 93, SEQ ID NO: 97, SEQ ID NO: 129, SEQ ID NO: 133 or SEQ ID NO:137; (iii) the full-length complement thereof; (iv) a subsequencethereof; (v) SEQ ID NO: 3, SEQ ID NO: 45, SEQ ID NO: 59, SEQ ID NO: 63,SEQ ID NO: 105, SEQ ID NO: 109, SEQ ID NO: 113, SEQ ID NO: 117, SEQ IDNO: 121, SEQ ID NO: 125; (vi) the mature polypeptide coding sequence ofSEQ ID NO: 3, SEQ ID NO: 45, SEQ ID NO: 59, SEQ ID NO: 63, SEQ ID NO:105, SEQ ID NO: 109, SEQ ID NO: 113, SEQ ID NO: 117, SEQ ID NO: 121, SEQID NO: 125; (vii) the full-length complement thereof; or (viii) asubsequence thereof; under medium stringency conditions to very highstringency conditions. Molecules to which the nucleic acid probehybridizes under these conditions can be detected using, for example,X-ray film or any other detection means known in the art.

In one aspect, the nucleic acid probe is a polynucleotide that encodesthe polypeptide of SEQ ID NO: 2, SEQ ID NO: 10, SEQ ID NO: 12, SEQ IDNO: 14, SEQ ID NO: 48, SEQ ID NO: 52, SEQ ID NO: 56, SEQ ID NO: 82, SEQID NO: 86, SEQ ID NO: 90, SEQ ID NO: 94, SEQ ID NO: 98, SEQ ID NO: 130,SEQ ID NO: 134 or SEQ ID NO: 138; the mature polypeptide thereof; or afragment thereof. In another aspect, the nucleic acid probe is SEQ IDNO: 1, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 47, SEQ IDNO: 51, SEQ ID NO: 55, SEQ ID NO: 81, SEQ ID NO: 85, SEQ ID NO: 89, SEQID NO: 93, SEQ ID NO: 97, SEQ ID NO: 129, SEQ ID NO: 133 or SEQ ID NO:137.

In one aspect, the nucleic acid probe is a polynucleotide that encodesthe polypeptide of SEQ ID NO: 4, SEQ ID NO: 46, SEQ ID NO: 60, SEQ IDNO: 64, SEQ ID NO: 106, SEQ ID NO: 110, SEQ ID NO: 114, SEQ ID NO: 118,SEQ ID NO: 122 or SEQ ID NO: 126; the mature polypeptide thereof; or afragment thereof. In another aspect, the nucleic acid probe is SEQ IDNO: 3, SEQ ID NO: 45, SEQ ID NO: 59, SEQ ID NO: 63, SEQ ID NO: 105, SEQID NO: 109, SEQ ID NO: 113, SEQ ID NO: 117, SEQ ID NO: 121 or SEQ ID NO:125.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 1 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 9 of at least 85%,e.g., at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 11 of at least 90%,e.g., at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 13 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 47 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 51 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 55 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 81 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 85 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 89 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 93 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 97 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 129 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 133 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolated GH9endoglucanase having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 137 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 3 of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 45 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 59 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 63 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 105 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 109 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 113 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 117 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 121 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to an isolatedpolypeptide having xanthan lyase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 125 of at least 80%, e.g., at least 85%, at least 86%, atleast 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 2 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 2 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acid changesmay be of a minor nature, that is conservative amino acid substitutionsor insertions that do not significantly affect the folding and/oractivity of the protein; small deletions, typically of 1-30 amino acids;small amino- or carboxyl-terminal extensions, such as an amino-terminalmethionine residue; a small linker peptide of up to 20-25 residues; or asmall extension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 4 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 4 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acid changesmay be of a minor nature, that is conservative amino acid substitutionsor insertions that do not significantly affect the folding and/oractivity of the protein; small deletions, typically of 1-30 amino acids;small amino- or carboxyl-terminal extensions, such as an amino-terminalmethionine residue; a small linker peptide of up to 20-25 residues; or asmall extension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 10 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 10 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 12 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 12 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 14 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 14 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 46 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 46 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 48 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 48 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 52 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 52 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 52 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 52 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 56 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 56 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 60 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 60 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 64 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 64 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 82 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 82 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 86 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 86 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 90 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 90 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 94 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 94 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 98 comprising a substitution, deletion,and/or insertion at one or more (e.g., several) positions. In anembodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 98 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 102 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 102 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 106 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 106 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 110 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 110 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 114 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 114 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 118 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 118 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 122 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 122 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 126 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 126 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas xanthan lyase activity.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 130 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 130 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 134 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 134 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to variants of themature polypeptide of SEQ ID NO: 138 comprising a substitution,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of amino acid substitutions, deletions and/orinsertions introduced into the mature polypeptide of SEQ ID NO: 138 isnot more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8 or 9. The amino acidchanges may be of a minor nature, that is conservative amino acidsubstitutions or insertions that do not significantly affect the foldingand/or activity of the protein; small deletions, typically of 1-30 aminoacids; small amino- or carboxyl-terminal extensions, such as anamino-terminal methionine residue; a small linker peptide of up to 20-25residues; or a small extension that facilitates purification by changingnet charge or another function, such as a His-tag (poly-histidinetract), an antigenic epitope or a binding domain. The variant preferablyhas activity on xanthan gum pre-treated with xanthan lyase.

Examples of conservative substitutions are within the groups of basicamino acids (arginine, lysine and histidine), acidic amino acids(glutamic acid and aspartic acid), polar amino acids (glutamine andasparagine), hydrophobic amino acids (leucine, isoleucine and valine),aromatic amino acids (phenylalanine, tryptophan and tyrosine), and smallamino acids (glycine, alanine, serine, threonine and methionine). Aminoacid substitutions that do not generally alter specific activity areknown in the art and are described, for example, by H. Neurath and R. L.Hill, 1979, In, The Proteins, Academic Press, New York. Commonsubstitutions are Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr,Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile,Leu/Val, Ala/Glu, and Asp/Gly.

Alternatively, the amino acid changes are of such a nature that thephysico-chemical properties of the polypeptides are altered. Forexample, amino acid changes may improve the thermal stability of thepolypeptide, alter the substrate specificity, change the pH optimum, andthe like.

Essential amino acids in a polypeptide can be identified according toprocedures known in the art, such as site-directed mutagenesis oralanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244:1081-1085). In the latter technique, single alanine mutations areintroduced at every residue in the molecule, and the resultant mutantmolecules are tested for cellulase and/or xanthan lyase activity toidentify amino acid residues that are critical to the activity of themolecule. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708.The active site of the enzyme or other biological interaction can alsobe determined by physical analysis of structure, as determined by suchtechniques as nuclear magnetic resonance, crystallography, electrondiffraction, or photoaffinity labelling, in conjunction with mutation ofputative contact site amino acids. See, for example, de Vos et al.,1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224:899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity ofessential amino acids can also be inferred from an alignment with arelated polypeptide.

Single or multiple amino acid substitutions, deletions, and/orinsertions can be made and tested using known methods of mutagenesis,recombination, and/or shuffling, followed by a relevant screeningprocedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988,Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA86: 2152-2156; WO 95/17413; or WO 95/22625. Other methods that can beused include error-prone PCR, phage display (e.g., Lowman et al., 1991,Biochemistry 30: 10832-10837; U.S. Pat. No. 5,223,409; WO 92/06204), andregion-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Neret al., 1988, DNA 7: 127).

Mutagenesis/shuffling methods can be combined with high-throughput,automated screening methods to detect activity of cloned, mutagenizedpolypeptides expressed by host cells (Ness et al., 1999, NatureBiotechnology 17: 893-896). Mutagenized DNA molecules that encode activepolypeptides can be recovered from the host cells and rapidly sequencedusing standard methods in the art. These methods allow the rapiddetermination of the importance of individual amino acid residues in apolypeptide.

The polypeptide may be a hybrid polypeptide in which a region of onepolypeptide is fused at the N-terminus or the C-terminus of a region ofanother polypeptide.

The polypeptide may be a fusion polypeptide or cleavable fusionpolypeptide in which another polypeptide is fused at the N-terminus orthe C-terminus of the polypeptide of the present invention. A fusionpolypeptide is produced by fusing a polynucleotide encoding anotherpolypeptide to a polynucleotide of the present invention. Techniques forproducing fusion polypeptides are known in the art, and include ligatingthe coding sequences encoding the polypeptides so that they are in frameand that expression of the fusion polypeptide is under control of thesame promoter(s) and terminator. Fusion polypeptides may also beconstructed using intein technology in which fusion polypeptides arecreated post-translationally (Cooper et al., 1993, EMBO J. 12:2575-2583; Dawson et al., 1994, Science 266: 776-779).

A fusion polypeptide can further comprise a cleavage site between thetwo polypeptides. Upon secretion of the fusion protein, the site iscleaved releasing the two polypeptides. Examples of cleavage sitesinclude, but are not limited to, the sites disclosed in Martin et al.,2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000,J. Biotechnol. 76: 245-251; Rasmussen-Wilson et al., 1997, Appl.Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13:498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton etal., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1995,Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure,Function, and Genetics 6: 240-248; and Stevens, 2003, Drug DiscoveryWorld 4: 35-48.

The polypeptide may be expressed by a recombinant DNA sequencecontaining the coding for a His-tag or HQ-tag to give, after anypost-translational modifications, the mature polypeptide containing allor part of the His- or HQ-tag. The HQ-tag, having the sequence -RHQHQHQ,may be fully or partly cleaved off the polypeptide during thepost-translational modifications resulting in for example the additionalamino acids -RHQHQ attached to the N-terminal of the mature polypeptide.The His-tag, having the sequence -RPHHHHHH, may be fully or partlycleaved off the polypeptide during the post-translational modificationsresulting in additional amino acids such as -RPHHHHH, -RPHHHH, -RPHHH,-RPHH, -RPH, -RP or -R attached to the N-terminal of the maturepolypeptide.

Compositions Comprising GH9 Endoglucanases Having Activity on XanthanGum Pretreated with Xanthan Lyase and Polypeptides Having Xanthan LyaseActivity

In an embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 2 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 2. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 2.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 2 or an allelic variant thereof; or is a fragment thereof havingendoglucanase activity and activity on xanthan gum pretreated withxanthan lyase. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 2. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 1055 of SEQ ID NO: 2.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 10 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 10. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 10.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 10 or an allelic variant thereof; or is a fragment thereof havingendoglucanase activity and having activity on xanthan gum pretreatedwith xanthan lyase. In another aspect, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 10. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 918 of SEQ ID NO: 10.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 12 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 12. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 12.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 12 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 12. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 916 of SEQ ID NO: 12.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 14 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 14. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 14.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 14 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 14. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 918 of SEQ ID NO: 14.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 48 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 48. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 48.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 48 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 48. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1007 of SEQ ID NO: 48.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 52 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 52. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 52.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 52 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 52. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 915 of SEQ ID NO: 52.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 56 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 56. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 56.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 56 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 56. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1056 of SEQ ID NO: 56.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 82 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 82. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 82.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 82 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 82. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1371 of SEQ ID NO: 82.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 86 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 86. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 86.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 86 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 86. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1203 of SEQ ID NO: 86.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 90 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 90. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 90.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 90 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 90. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1379 of SEQ ID NO: 90.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 94 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 94. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 94.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 94 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 94. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1371 of SEQ ID NO: 94.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 98 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 98. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 98.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 98 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 98. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1372 of SEQ ID NO: 98.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 102 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.The composition is preferably a detergent composition comprising one ormore detergent components as defined herein, and may be used for washingor cleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 102. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 102.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 102 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 102. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 922 of SEQ ID NO: 102.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 130 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.The composition is preferably a detergent composition comprising one ormore detergent components as defined herein, and may be used for washingor cleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

An embodiment of the invention is a composition comprising isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase and having a sequence identity to the mature polypeptide of SEQ IDNO: 130 of at least 85%.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 130. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 130.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 130 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 130. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 916 of SEQ ID NO: 130.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 134 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.The composition is preferably a detergent composition comprising one ormore detergent components as defined herein, and may be used for washingor cleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 134. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 134.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 134 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 134. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1373 of SEQ ID NO: 134.

In a further embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase and having a sequence identity to themature polypeptide of SEQ ID NO: 138 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.The composition is preferably a detergent composition comprising one ormore detergent components as defined herein, and may be used for washingor cleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 138. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 138.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 138 or an allelic variant thereof; or is a fragment thereof havingactivity on xanthan gum pretreated with xanthan lyase. In anotheraspect, the composition comprises a polypeptide that comprises orconsists of the mature polypeptide of SEQ ID NO: 138. In another aspect,the composition comprises a polypeptide that comprises or consists ofamino acids 1 to 1204 of SEQ ID NO: 138.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide thathybridizes under medium stringency conditions, medium-high stringencyconditions, high stringency conditions, or very high stringencyconditions with the mature polypeptide coding sequence of SEQ ID NO: 1,SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 47, SEQ ID NO:51, SEQ ID NO: 55, SEQ ID NO: 81, SEQ ID NO: 85, SEQ ID NO: 89, SEQ IDNO: 93, SEQ ID NO: 97, SEQ ID NO: 129, SEQ ID NO: 133, SEQ ID NO: 137,or the full-length complement thereof (Sambrook et al., 1989, MolecularCloning, A Laboratory Manual, 2d edition, Cold Spring Harbor, N.Y.). Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity andhaving a sequence identity to the mature polypeptide of SEQ ID NO: 4 ofat least 80%, e.g., at least 85%, at least 86%, at least 87%, at least88%, at least 89%, at least 90%, at least 91%, at least 92%, at least93%, at least 94%, at least 95%, at least 96%, at least 97%, at least98%, at least 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 4. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 4.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 4 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 4. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 760 of SEQ ID NO: 4.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 46 of at least80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%, atleast 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 46. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 46.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 46 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 46. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 1043 of SEQ ID NO: 46.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 60 of at least80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%, atleast 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 60. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 60.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 60 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 60. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 896 of SEQ ID NO: 60.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 64 of at least80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%, atleast 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 64. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 64.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 64 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 64. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 1038 of SEQ ID NO: 64.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 106 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 106. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 106.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 106 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 106. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 901 of SEQ ID NO: 106.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 110 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 110. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 110.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 110 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 110. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 899 of SEQ ID NO: 110.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 114 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 114. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 114.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 114 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 114. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 897 of SEQ ID NO: 114.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 118 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 118. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 118.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 118 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 118. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 933 of SEQ ID NO: 118.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 122 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 122. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 122.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 122 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 122. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 1049 of SEQ ID NO: 122.

In an embodiment, the present invention relates to a compositioncomprising isolated polypeptides having lyase activity and having asequence identity to the mature polypeptide of SEQ ID NO: 126 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In one aspect, the polypeptides differ by no more than 50 amino acids,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, or 49, from the maturepolypeptide of SEQ ID NO: 126. In a preferred aspect, the polypeptidesdiffer by no more than 10 amino acids, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9or 10 amino acids, from the mature polypeptide of SEQ ID NO: 126.

A composition comprising a polypeptide of the present inventionpreferably comprises or consists of the amino acid sequence of SEQ IDNO: 126 or an allelic variant thereof; or is a fragment thereof havingxanthan lyase activity. In another aspect, the composition comprises apolypeptide that comprises or consists of the mature polypeptide of SEQID NO: 126. In another aspect, the composition comprises a polypeptidethat comprises or consists of amino acids 1 to 900 of SEQ ID NO: 126.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide that hybridizes under medium stringency conditions,medium-high stringency conditions, high stringency conditions, or veryhigh stringency conditions with the mature polypeptide coding sequenceof SEQ ID NO: 3, SEQ ID NO: 45, SEQ ID NO: 59, SEQ ID NO: 63, SEQ ID NO:105, SEQ ID NO: 109, SEQ ID NO: 113, SEQ ID NO: 117, SEQ ID NO: 121, SEQID NO: 125, or the full-length complement thereof (Sambrook et al.,1989, Molecular Cloning, A Laboratory Manual, 2d edition, Cold SpringHarbor, N.Y.). The composition is preferably a detergent compositioncomprising one or more detergent components as defined herein, and maybe used for washing or cleaning a textile and/or a hard surface such asdish wash. Alternatively, the composition may be used for degradingxanthan gum such as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 1 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 9 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 11 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to an isolated GH9endoglucanases having activity on xanthan gum pretreated with xanthanlyase encoded by a polynucleotide having a sequence identity to themature polypeptide coding sequence of SEQ ID NO: 13 of at least 80%,e.g., of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 47 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 51 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 55 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 81 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 85 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 89 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 93 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 97 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 101 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 129 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 133 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated GH9 endoglucanases having activity on xanthan gumpretreated with xanthan lyase encoded by a polynucleotide having asequence identity to the mature polypeptide coding sequence of SEQ IDNO: 137 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%. The composition is preferably adetergent composition comprising one or more detergent components asdefined herein, and may be used for washing or cleaning a textile and/ora hard surface such as dish wash. Alternatively, the composition may beused for degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 3 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 45 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 59 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 63 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 105 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 109 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 113 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 117 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 121 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to a compositioncomprising isolated polypeptides having xanthan lyase activity encodedby a polynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 125 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. Thecomposition is preferably a detergent composition comprising one or moredetergent components as defined herein, and may be used for washing orcleaning a textile and/or a hard surface such as dish wash.Alternatively, the composition may be used for degrading xanthan gumsuch as for controlling the viscosity of drilling fluids.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 2 comprisinga substitution, deletion, and/or insertion at one or more (e.g.,several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 2 is not more than 10, e.g., 1, 2, 3, 4, 5, 6,7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 4 comprisinga substitution, deletion, and/or insertion at one or more (e.g.,several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 4 is not more than 10, e.g., 1, 2, 3, 4, 5, 6,7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 10comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 10 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 12comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 12 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 14comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 14 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 46comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 46 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 48comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 48 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 52comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 52 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 56comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 56 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 60comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 60 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 64comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 64 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 82comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 82 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 86comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 86 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 90comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 90 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 94comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 94 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 98comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 98 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 102comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 102 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 106comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 106 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 110comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 110 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 114comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 114 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 118comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 118 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 122comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 122 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 126comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 126 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has xanthan lyaseactivity.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 130comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 130 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 134comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 134 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

In another embodiment, the present invention relates to compositionscomprising variants of the mature polypeptide of SEQ ID NO: 138comprising a substitution, deletion, and/or insertion at one or more(e.g., several) positions. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. In an embodiment, the number of amino acidsubstitutions, deletions and/or insertions introduced into the maturepolypeptide of SEQ ID NO: 138 is not more than 10, e.g., 1, 2, 3, 4, 5,6, 7, 8 or 9. The amino acid changes may be of a minor nature, that isconservative amino acid substitutions or insertions that do notsignificantly affect the folding and/or activity of the protein; smalldeletions, typically of 1-30 amino acids; small amino- orcarboxyl-terminal extensions, such as an amino-terminal methionineresidue; a small linker peptide of up to 20-25 residues; or a smallextension that facilitates purification by changing net charge oranother function, such as a His-tag (poly-histidine tract), an antigenicepitope or a binding domain. The variant preferably has activity onxanthan gum pre-treated with xanthan lyase.

Examples of conservative substitutions are within the groups of basicamino acids (arginine, lysine and histidine), acidic amino acids(glutamic acid and aspartic acid), polar amino acids (glutamine andasparagine), hydrophobic amino acids (leucine, isoleucine and valine),aromatic amino acids (phenylalanine, tryptophan and tyrosine), and smallamino acids (glycine, alanine, serine, threonine and methionine). Aminoacid substitutions that do not generally alter specific activity areknown in the art and are described, for example, by H. Neurath and R. L.Hill, 1979, In, The Proteins, Academic Press, New York. Commonsubstitutions are Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr,Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile,Leu/Val, Ala/Glu, and Asp/Gly.

Alternatively, the amino acid changes are of such a nature that thephysico-chemical properties of the polypeptides are altered. Forexample, amino acid changes may improve the thermal stability of thepolypeptide, alter the substrate specificity, change the pH optimum, andthe like.

Essential amino acids in a polypeptide can be identified according toprocedures known in the art, such as site-directed mutagenesis oralanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244:1081-1085). In the latter technique, single alanine mutations areintroduced at every residue in the molecule, and the resultant mutantmolecules are tested for cellulase and/or xanthan lyase activity toidentify amino acid residues that are critical to the activity of themolecule. See also, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708.The active site of the enzyme or other biological interaction can alsobe determined by physical analysis of structure, as determined by suchtechniques as nuclear magnetic resonance, crystallography, electrondiffraction, or photoaffinity labelling, in conjunction with mutation ofputative contact site amino acids. See, for example, de Vos et al.,1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224:899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity ofessential amino acids can also be inferred from an alignment with arelated polypeptide.

Single or multiple amino acid substitutions, deletions, and/orinsertions can be made and tested using known methods of mutagenesis,recombination, and/or shuffling, followed by a relevant screeningprocedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988,Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA86: 2152-2156; WO 95/17413; or WO 95/22625. Other methods that can beused include error-prone PCR, phage display (e.g., Lowman et al., 1991,Biochemistry 30: 10832-10837; U.S. Pat. No. 5,223,409; WO 92/06204), andregion-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Neret al., 1988, DNA 7: 127).

Mutagenesis/shuffling methods can be combined with high-throughput,automated screening methods to detect activity of cloned, mutagenizedpolypeptides expressed by host cells (Ness et al., 1999, NatureBiotechnology 17: 893-896). Mutagenized DNA molecules that encode activepolypeptides can be recovered from the host cells and rapidly sequencedusing standard methods in the art. These methods allow the rapiddetermination of the importance of individual amino acid residues in apolypeptide.

Embodiments

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids. An embodiment of the invention is a compositioncomprising the GH9 endoglucanase of SEQ ID NO: 2 with a polypeptidehaving xanthan lyase activity of SEQ ID NO: 46. The composition ispreferably a detergent composition comprising one or more detergentcomponents as defined herein, and may be used for washing or cleaning atextile and/or a hard surface such as dish wash. Alternatively, thecomposition may be used for degrading xanthan gum such as forcontrolling the viscosity of drilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 2 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 10 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 12 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 14 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 48 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 52 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 56 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 82 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 86 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 90 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 94 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 98 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 102 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 130 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 134 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 4. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 46. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 60. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 64. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 106. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 110. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 114. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 118. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 122. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

An embodiment of the invention is a composition comprising the GH9endoglucanase of SEQ ID NO: 138 with a polypeptide having xanthan lyaseactivity of SEQ ID NO: 126. The composition is preferably a detergentcomposition comprising one or more detergent components as definedherein, and may be used for washing or cleaning a textile and/or a hardsurface such as dish wash. Alternatively, the composition may be usedfor degrading xanthan gum such as for controlling the viscosity ofdrilling fluids.

Sources of GH9 Endoglucanases Having Activity on Xanthan Gum Pretreatedwith Xanthan Lyase and Polypeptides Having Xanthan Lyase Activity

A GH9 endoglucanase having activity on xanthan gum pretreated with axanthan lyase of the present invention and polypeptides having xanthanlyase activity may be obtained from microorganisms of any genus. Forpurposes of the present invention, the term “obtained from” as usedherein in connection with a given source shall mean that the polypeptideencoded by a polynucleotide is produced by the source or by a strain inwhich the polynucleotide from the source has been inserted. In oneaspect, the polypeptide obtained from a given source is secretedextracellularly.

In one aspect, the polypeptide is from a bacterium of the class Bacilli,such as from the order Bacillales, or from the family Paenibacillaceae,or from the genus Paeniobacillus or from the species Paeniobacillus suchas Paeniobacillus sp NN062047, Paeniobacillus sp NN062250,Paeniobacillus sp NN062253, Paeniobacillus sp NN018054, Paeniobacillussp NN062046, Paeniobacillus sp NN062408, Paeniobacillus sp NN062332,Paeniobacillus sp NN062147 or Paeniobacillus sp NN062193.

In another aspect, the polypeptide from a bacterium of the classActinobacteria, such as from the order Actinomycetales, or from thefamily Microbacteriaceae, or from the genus Microbacterium or from thespecies Microbacterium such as Microbacterium testaceum, Microbacteriumsp NN062045, Microbacterium sp NN062148, Microbacterium sp NN062175 orMicrobacterium sp NN062149.

It will be understood that for the aforementioned species, the inventionencompasses both the perfect and imperfect states, and other taxonomicequivalents, e.g., anamorphs, regardless of the species name by whichthey are known. Those skilled in the art will readily recognize theidentity of appropriate equivalents.

Strains of these species are readily accessible to the public in anumber of culture collections, such as the American Type CultureCollection (ATCC), Deutsche Sammlung von Mikroorganismen andZellkulturen GmbH (DSMZ), Centraalbureau Voor Schimmelcultures (CBS),and Agricultural Research Service Patent Culture Collection, NorthernRegional Research Center (NRRL).

The polypeptide may be identified and obtained from other sourcesincluding microorganisms isolated from nature (e.g., soil, composts,water, etc.) or DNA samples obtained directly from natural materials(e.g., soil, composts, water, etc.) using the above-mentioned probes.Techniques for isolating microorganisms and DNA directly from naturalhabitats are well known in the art. A polynucleotide encoding thepolypeptide may then be obtained by similarly screening a genomic DNA orcDNA library of another microorganism or mixed DNA sample. Once apolynucleotide encoding a polypeptide has been detected with theprobe(s), the polynucleotide can be isolated or cloned by utilizingtechniques that are known to those of ordinary skill in the art (see,e.g., Sambrook et al., 1989, supra).

Polynucleotides

The present invention also relates to isolated polynucleotides encodinga polypeptide of the present invention, as described herein.

The techniques used to isolate or clone a polynucleotide are known inthe art and include isolation from genomic DNA or cDNA, or a combinationthereof. The cloning of the polynucleotides from genomic DNA can beeffected, e.g., by using the well known polymerase chain reaction (PCR)or antibody screening of expression libraries to detect cloned DNAfragments with shared structural features. See, e.g., Innis et al.,1990, PCR: A Guide to Methods and Application, Academic Press, New York.Other nucleic acid amplification procedures such as ligase chainreaction (LCR), ligation activated transcription (LAT) andpolynucleotide-based amplification (NASBA) may be used. Thepolynucleotides may be cloned in a strain of Bacillus subtilis or E.Coli, or a related organism and thus, for example, may be an allelic orspecies variant of the polypeptide encoding region of thepolynucleotide.

Modification of a polynucleotide encoding a polypeptide of the presentinvention may be necessary for synthesizing polypeptides substantiallysimilar to the polypeptide. The term “substantially similar” to thepolypeptide refers to non-naturally occurring forms of the polypeptide.These polypeptides may differ in some engineered way from thepolypeptide isolated from its native source, e.g., variants that differin specific activity, thermostability, pH optimum, or the like. Thevariants may be constructed on the basis of the polynucleotide presentedas the mature polypeptide coding sequence of SEQ ID NO: 1, SEQ ID NO: 3,SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID: NO:13, SEQ ID NO: 15, SEQ ID NO:45, SEQ ID NO: 47, SEQ ID NO: 51, SEQ ID NO: 55, SEQ ID NO: 59, SEQ IDNO: 63, SEQ ID NO: 81, SEQ ID NO: 85, SEQ ID NO: 89, SEQ ID NO: 93, SEQID NO: 97, SEQ ID NO: 105, SEQ ID NO: 109, SEQ ID NO: 113, SEQ ID NO:117, SEQ ID NO: 121, SEQ ID NO: 125, SEQ ID NO: 129, SEQ ID NO: 133 orSEQ ID NO: 137 e.g., a subsequence thereof, and/or by introduction ofnucleotide substitutions that do not result in a change in the aminoacid sequence of the polypeptide, but which correspond to the codonusage of the host organism intended for production of the enzyme, or byintroduction of nucleotide substitutions that may give rise to adifferent amino acid sequence. For a general description of nucleotidesubstitution, see, Ford et al., (1991), ‘Protein Expression andPurification’, 2: 95-107.

Nucleic Acid Constructs

The present invention also relates to nucleic acid constructs comprisinga polynucleotide of the present invention operably linked to one or morecontrol sequences that direct the expression of the coding sequence in asuitable host cell under conditions compatible with the controlsequences.

A polynucleotide may be manipulated in a variety of ways to provide forexpression of the polypeptide. Manipulation of the polynucleotide priorto its insertion into a vector may be desirable or necessary dependingon the expression vector. The techniques for modifying polynucleotidesutilizing recombinant DNA methods are well known in the art.

The control sequence may be a promoter, a polynucleotide that isrecognized by a host cell for expression of a polynucleotide encoding apolypeptide of the present invention. The promoter containstranscriptional control sequences that mediate the expression of thepolypeptide. The promoter may be any polynucleotide that showstranscriptional activity in the host cell including mutant, truncated,and hybrid promoters, and may be obtained from genes encodingextracellular or intracellular polypeptides either homologous orheterologous to the host cell.

Examples of suitable promoters for directing transcription of thenucleic acid constructs of the present invention in a bacterial hostcell are the promoters obtained from the Bacillus amyloliquefaciensalpha-amylase gene (amyQ), Bacillus licheniformis alpha-amylase gene(amyL), Bacillus licheniformis penicillinase gene (penP), Bacillusstearothermophilus maltogenic amylase gene (amyM), Bacillus subtilislevansucrase gene (sacB), Bacillus subtilis xylA and xylB genes,Bacillus thuringiensis cryIIIA gene (Agaisse and Lereclus, 1994,Molecular Microbiology 13: 97-107), E. coli lac operon, E. coli trcpromoter (Egon et al., 1988, Gene 69: 301-315), Streptomyces coelicoloragarase gene (dagA), and prokaryotic beta-lactamase gene (Villa-Kamaroffet al., 1978, Proc. Natl. Acad. Sci. USA 75: 3727-3731), as well as thetac promoter (DeBoer et al., 1983, Proc. Natl. Acad. Sci. USA 80:21-25). Further promoters are described in “Useful proteins fromrecombinant bacteria” in Gilbert et al., 1980, Scientific American 242:74-94; and in Sambrook et al., 1989, supra. Examples of tandem promotersare disclosed in WO 99/43835.

Examples of suitable promoters for directing transcription of thenucleic acid constructs of the present invention in a filamentous fungalhost cell are promoters obtained from the genes for Aspergillus nidulansacetamidase, Aspergillus niger neutral alpha-amylase, Aspergillus nigeracid stable alpha-amylase, Aspergillus niger or Aspergillus awamoriglucoamylase (glaA), Aspergillus oryzae TAKA amylase, Aspergillus oryzaealkaline protease, Aspergillus oryzae triose phosphate isomerase,Fusarium oxysporum trypsin-like protease (WO 96/00787), Fusariumvenenatum amyloglucosidase (WO 00/56900), Fusarium venenatum Daria (WO00/56900), Fusarium venenatum Quinn (WO 00/56900), Rhizomucor mieheilipase, Rhizomucor miehei aspartic proteinase, Trichoderma reeseibeta-glucosidase, Trichoderma reesei cellobiohydrolase I, Trichodermareesei cellobiohydrolase II, Trichoderma reesei endoglucanase I,Trichoderma reesei endoglucanase II, Trichoderma reesei endoglucanaseIII, Trichoderma reesei endoglucanase IV, Trichoderma reeseiendoglucanase V, Trichoderma reesei xylanase I, Trichoderma reeseixylanase II, Trichoderma reesei beta-xylosidase, as well as the NA2-tpipromoter (a modified promoter from an Aspergillus neutral alpha-amylasegene in which the untranslated leader has been replaced by anuntranslated leader from an Aspergillus triose phosphate isomerase gene;non-limiting examples include modified promoters from an Aspergillusniger neutral alpha-amylase gene in which the untranslated leader hasbeen replaced by an untranslated leader from an Aspergillus nidulans orAspergillus oryzae triose phosphate isomerase gene); and mutant,truncated, and hybrid promoters thereof.

In a yeast host, useful promoters are obtained from the genes forSaccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiaegalactokinase (GAL1), Saccharomyces cerevisiae alcoholdehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH1, ADH2/GAP),Saccharomyces cerevisiae triose phosphate isomerase (TPI), Saccharomycescerevisiae metallothionein (CUP1), and Saccharomyces cerevisiae3-phosphoglycerate kinase. Other useful promoters for yeast host cellsare described by Romanos et al., 1992, Yeast 8: 423-488.

The control sequence may also be a transcription terminator, which isrecognized by a host cell to terminate transcription. The terminator isoperably linked to the 3′-terminus of the polynucleotide encoding thepolypeptide. Any terminator that is functional in the host cell may beused in the present invention.

Preferred terminators for bacterial host cells are obtained from thegenes for Bacillus clausii alkaline protease (aprH), Bacilluslicheniformis alpha-amylase (amyL), and Escherichia coli ribosomal RNA(rrnB).

Preferred terminators for filamentous fungal host cells are obtainedfrom the genes for Aspergillus nidulans anthranilate synthase,Aspergillus niger glucoamylase, Aspergillus niger alpha-glucosidase,Aspergillus oryzae TAKA amylase, and Fusarium oxysporum trypsin-likeprotease.

Preferred terminators for yeast host cells are obtained from the genesfor Saccharomyces cerevisiae enolase, Saccharomyces cerevisiaecytochrome C (CYC1), and Saccharomyces cerevisiaeglyceraldehyde-3-phosphate dehydrogenase. Other useful terminators foryeast host cells are described by Romanos et al., 1992, supra.

The control sequence may also be an mRNA stabilizer region downstream ofa promoter and upstream of the coding sequence of a gene which increasesexpression of the gene.

Examples of suitable mRNA stabilizer regions are obtained from aBacillus thuringiensis cryIIIA gene (WO 94/25612) and a Bacillussubtilis SP82 gene (Hue et al., 1995, Journal of Bacteriology 177:3465-3471).

The control sequence may also be a leader, a nontranslated region of anmRNA that is important for translation by the host cell. The leader isoperably linked to the 5′-terminus of the polynucleotide encoding thepolypeptide. Any leader that is functional in the host cell may be used.

Preferred leaders for filamentous fungal host cells are obtained fromthe genes for Aspergillus oryzae TAKA amylase and Aspergillus nidulanstriose phosphate isomerase.

Suitable leaders for yeast host cells are obtained from the genes forSaccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae3-phosphoglycerate kinase, Saccharomyces cerevisiae alpha-factor, andSaccharomyces cerevisiae alcoholdehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP).

The control sequence may also be a polyadenylation sequence, a sequenceoperably linked to the 3′-terminus of the polynucleotide and, whentranscribed, is recognized by the host cell as a signal to addpolyadenosine residues to transcribed mRNA. Any polyadenylation sequencethat is functional in the host cell may be used.

Preferred polyadenylation sequences for filamentous fungal host cellsare obtained from the genes for Aspergillus nidulans anthranilatesynthase, Aspergillus niger glucoamylase, Aspergillus nigeralpha-glucosidase Aspergillus oryzae TAKA amylase, and Fusariumoxysporum trypsin-like protease.

Useful polyadenylation sequences for yeast host cells are described byGuo and Sherman, 1995, Mol. Cellular Biol. 15: 5983-5990.

The control sequence may also be a signal peptide coding region thatencodes a signal peptide linked to the N-terminus of a polypeptide anddirects the polypeptide into the cell's secretory pathway. The 5′-end ofthe coding sequence of the polynucleotide may inherently contain asignal peptide coding sequence naturally linked in translation readingframe with the segment of the coding sequence that encodes thepolypeptide. Alternatively, the 5′-end of the coding sequence maycontain a signal peptide coding sequence that is foreign to the codingsequence. A foreign signal peptide coding sequence may be required wherethe coding sequence does not naturally contain a signal peptide codingsequence. Alternatively, a foreign signal peptide coding sequence maysimply replace the natural signal peptide coding sequence in order toenhance secretion of the polypeptide. However, any signal peptide codingsequence that directs the expressed polypeptide into the secretorypathway of a host cell may be used.

Effective signal peptide coding sequences for bacterial host cells arethe signal peptide coding sequences obtained from the genes for BacillusNCIB 11837 maltogenic amylase, Bacillus licheniformis subtilisin,Bacillus licheniformis beta-lactamase, Bacillus stearothermophilusalpha-amylase, Bacillus stearothermophilus neutral proteases (nprT,nprS, nprM), and Bacillus subtilis prsA. Further signal peptides aredescribed by Simonen and Palva, 1993, Microbiological Reviews 57:109-137.

Effective signal peptide coding sequences for filamentous fungal hostcells are the signal peptide coding sequences obtained from the genesfor Aspergillus niger neutral amylase, Aspergillus niger glucoamylase,Aspergillus oryzae TAKA amylase, Humicola insolens cellulase, Humicolainsolens endoglucanase V, Humicola lanuginosa lipase, and Rhizomucormiehei aspartic proteinase.

Useful signal peptides for yeast host cells are obtained from the genesfor Saccharomyces cerevisiae alpha-factor and Saccharomyces cerevisiaeinvertase. Other useful signal peptide coding sequences are described byRomanos et al., 1992, supra.

The control sequence may also be a propeptide coding sequence thatencodes a propeptide positioned at the N-terminus of a polypeptide. Theresultant polypeptide is known as a proenzyme or propolypeptide (or azymogen in some cases). A propolypeptide is generally inactive and canbe converted to an active polypeptide by catalytic or autocatalyticcleavage of the propeptide from the propolypeptide. The propeptidecoding sequence may be obtained from the genes for Bacillus subtilisalkaline protease (aprE), Bacillus subtilis neutral protease (nprT),Myceliophthora thermophila laccase (WO 95/33836), Rhizomucor mieheiaspartic proteinase, and Saccharomyces cerevisiae alpha-factor.

Where both signal peptide and propeptide sequences are present, thepropeptide sequence is positioned next to the N-terminus of apolypeptide and the signal peptide sequence is positioned next to theN-terminus of the propeptide sequence.

It may also be desirable to add regulatory sequences that regulateexpression of the polypeptide relative to the growth of the host cell.Examples of regulatory systems are those that cause expression of thegene to be turned on or off in response to a chemical or physicalstimulus, including the presence of a regulatory compound. Regulatorysystems in prokaryotic systems include the lac, tac, and trp operatorsystems. In yeast, the ADH2 system or GAL1 system may be used. Infilamentous fungi, the Aspergillus niger glucoamylase promoter,Aspergillus oryzae TAKA alpha-amylase promoter, and Aspergillus oryzaeglucoamylase promoter may be used. Other examples of regulatorysequences are those that allow for gene amplification. In eukaryoticsystems, these regulatory sequences include the dihydrofolate reductasegene that is amplified in the presence of methotrexate, and themetallothionein genes that are amplified with heavy metals. In thesecases, the polynucleotide encoding the polypeptide would be operablylinked with the regulatory sequence.

Expression Vectors

The present invention also relates to recombinant expression vectorscomprising a polynucleotide of the present invention, a promoter, andtranscriptional and translational stop signals. The various nucleotideand control sequences may be joined together to produce a recombinantexpression vector that may include one or more convenient restrictionsites to allow for insertion or substitution of the polynucleotideencoding the polypeptide at such sites. Alternatively, thepolynucleotide may be expressed by inserting the polynucleotide or anucleic acid construct comprising the polynucleotide into an appropriatevector for expression. In creating the expression vector, the codingsequence is located in the vector so that the coding sequence isoperably linked with the appropriate control sequences for expression.

The recombinant expression vector may be any vector (e.g., a plasmid orvirus) that can be conveniently subjected to recombinant DNA proceduresand can bring about expression of the polynucleotide. The choice of thevector will typically depend on the compatibility of the vector with thehost cell into which the vector is to be introduced. The vector may be alinear or closed circular plasmid.

The vector may be an autonomously replicating vector, i.e., a vectorthat exists as an extrachromosomal entity, the replication of which isindependent of chromosomal replication, e.g., a plasmid, anextrachromosomal element, a minichromosome, or an artificial chromosome.The vector may contain any means for assuring self-replication.Alternatively, the vector may be one that, when introduced into the hostcell, is integrated into the genome and replicated together with thechromosome(s) into which it has been integrated. Furthermore, a singlevector or plasmid or two or more vectors or plasmids that togethercontain the total DNA to be introduced into the genome of the host cell,or a transposon, may be used.

The vector preferably contains one or more selectable markers thatpermit easy selection of transformed, transfected, transduced, or thelike cells. A selectable marker is a gene the product of which providesfor biocide or viral resistance, resistance to heavy metals, prototrophyto auxotrophs, and the like.

Examples of bacterial selectable markers are Bacillus licheniformis orBacillus subtilis dal genes, or markers that confer antibioticresistance such as ampicillin, chloramphenicol, kanamycin, neomycin,spectinomycin, or tetracycline resistance. Suitable markers for yeasthost cells include, but are not limited to, ADE2, HIS3, LEU2, LYS2,MET3, TRP1, and URA3. Selectable markers for use in a filamentous fungalhost cell include, but are not limited to, amdS (acetamidase), argB(ornithine carbamoyltransferase), bar (phosphinothricinacetyltransferase), hph (hygromycin phosphotransferase), niaD (nitratereductase), pyrG (orotidine-5′-phosphate decarboxylase), sC (sulfateadenyltransferase), and trpC (anthranilate synthase), as well asequivalents thereof. Preferred for use in an Aspergillus cell areAspergillus nidulans or Aspergillus oryzae amdS and pyrG genes and aStreptomyces hygroscopicus bar gene.

The vector preferably contains an element(s) that permits integration ofthe vector into the host cell's genome or autonomous replication of thevector in the cell independent of the genome.

For integration into the host cell genome, the vector may rely on thepolynucleotide's sequence encoding the polypeptide or any other elementof the vector for integration into the genome by homologous ornon-homologous recombination. Alternatively, the vector may containadditional polynucleotides for directing integration by homologousrecombination into the genome of the host cell at a precise location(s)in the chromosome(s). To increase the likelihood of integration at aprecise location, the integrational elements should contain a sufficientnumber of nucleic acids, such as 100 to 10,000 base pairs, 400 to 10,000base pairs, and 800 to 10,000 base pairs, which have a high degree ofsequence identity to the corresponding target sequence to enhance theprobability of homologous recombination. The integrational elements maybe any sequence that is homologous with the target sequence in thegenome of the host cell. Furthermore, the integrational elements may benon-encoding or encoding polynucleotides. On the other hand, the vectormay be integrated into the genome of the host cell by non-homologousrecombination.

For autonomous replication, the vector may further comprise an origin ofreplication enabling the vector to replicate autonomously in the hostcell in question. The origin of replication may be any plasmidreplicator mediating autonomous replication that functions in a cell.The term “origin of replication” or “plasmid replicator” means apolynucleotide that enables a plasmid or vector to replicate in vivo.

Examples of bacterial origins of replication are the origins ofreplication of plasmids pBR322, pUC19, pACYC177, and pACYC184 permittingreplication in E. coli, and pUB110, pE194, pTA1060, and pAMβ1 permittingreplication in Bacillus.

Examples of origins of replication for use in a yeast host cell are the2 micron origin of replication, ARS1, ARS4, the combination of ARS1 andCEN3, and the combination of ARS4 and CEN6.

Examples of origins of replication useful in a filamentous fungal cellare AMA1 and ANS1 (Gems et al., 1991, Gene 98: 61-67; Cullen et al.,1987, Nucleic Acids Res. 15: 9163-9175; WO 00/24883). Isolation of theAMA1 gene and construction of plasmids or vectors comprising the genecan be accomplished according to the methods disclosed in WO 00/24883.

More than one copy of a polynucleotide of the present invention may beinserted into a host cell to increase production of a polypeptide. Anincrease in the copy number of the polynucleotide can be obtained byintegrating at least one additional copy of the sequence into the hostcell genome or by including an amplifiable selectable marker gene withthe polynucleotide where cells containing amplified copies of theselectable marker gene, and thereby additional copies of thepolynucleotide, can be selected for by cultivating the cells in thepresence of the appropriate selectable agent.

The procedures used to ligate the elements described above to constructthe recombinant expression vectors of the present invention are wellknown to one skilled in the art (see, e.g., Sambrook et al., 1989,supra).

Host Cells

The present invention also relates to recombinant host cells, comprisinga polynucleotide of the present invention operably linked to one or morecontrol sequences that direct the production of a polypeptide of thepresent invention. A construct or vector comprising a polynucleotide isintroduced into a host cell so that the construct or vector ismaintained as a chromosomal integrant or as a self-replicatingextra-chromosomal vector as described earlier. The term “host cell”encompasses any progeny of a parent cell that is not identical to theparent cell due to mutations that occur during replication. The choiceof a host cell will to a large extent depend upon the gene encoding thepolypeptide and its source.

The host cell may be any cell useful in the recombinant production of apolypeptide of the present invention, e.g., a prokaryote or a eukaryote.

The prokaryotic host cell may be any Gram-positive or Gram-negativebacterium. Gram-positive bacteria include, but are not limited to,Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus,Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, andStreptomyces. Gram-negative bacteria include, but are not limited to,Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter,Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.

The bacterial host cell may be any Bacillus cell including, but notlimited to, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillusbrevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans,Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacilluslicheniformis, Bacillus megaterium, Bacillus pumilus, Bacillusstearothermophilus, Bacillus subtilis, and Bacillus thuringiensis cells.

The bacterial host cell may also be any Streptococcus cell including,but not limited to, Streptococcus equisimilis, Streptococcus pyogenes,Streptococcus uberis, and Streptococcus equi subsp. Zooepidemicus cells.

The bacterial host cell may also be any Streptomyces cell including, butnot limited to, Streptomyces achromogenes, Streptomyces avermitilis,Streptomyces coelicolor, Streptomyces griseus, and Streptomyces lividanscells.

The introduction of DNA into a Bacillus cell may be effected byprotoplast transformation (see, e.g., Chang and Cohen, 1979, Mol. Gen.Genet. 168: 111-115), competent cell transformation (see, e.g., Youngand Spizizen, 1961, J. Bacteriol. 81: 823-829, or Dubnau andDavidoff-Abelson, 1971, J. Mol. Biol. 56: 209-221), electroporation(see, e.g., Shigekawa and Dower, 1988, Biotechniques 6: 742-751), orconjugation (see, e.g., Koehler and Thorne, 1987, J. Bacteriol. 169:5271-5278). The introduction of DNA into an E. coli cell may be effectedby protoplast transformation (see, e.g., Hanahan, 1983, J. Mol. Biol.166: 557-580) or electroporation (see, e.g., Dower et al., 1988, NucleicAcids Res. 16: 6127-6145). The introduction of DNA into a Streptomycescell may be effected by protoplast transformation, electroporation (see,e.g., Gong et al., 2004, Folia Microbiol. (Praha) 49: 399-405),conjugation (see, e.g., Mazodier et al., 1989, J. Bacteriol. 171:3583-3585), or transduction (see, e.g., Burke et al., 2001, Proc. Natl.Acad. Sci. USA 98: 6289-6294). The introduction of DNA into aPseudomonas cell may be effected by electroporation (see, e.g., Choi etal., 2006, J. Microbiol. Methods 64: 391-397) or conjugation (see, e.g.,Pinedo and Smets, 2005, Appl. Environ. Microbiol. 71: 51-57). Theintroduction of DNA into a Streptococcus cell may be effected by naturalcompetence (see, e.g., Perry and Kuramitsu, 1981, Infect. Immun. 32:1295-1297), protoplast transformation (see, e.g., Catt and Jollick,1991, Microbios 68: 189-207), electroporation (see, e.g., Buckley etal., 1999, Appl. Environ. Microbiol. 65: 3800-3804), or conjugation(see, e.g., Clewell, 1981, Microbiol. Rev. 45: 409-436). However, anymethod known in the art for introducing DNA into a host cell can beused.

The host cell may also be a eukaryote, such as a mammalian, insect,plant, or fungal cell.

The host cell may be a fungal cell. “Fungi” as used herein includes thephyla Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota as wellas the Oomycota and all mitosporic fungi (as defined by Hawksworth etal., In, Ainsworth and Bisby's Dictionary of The Fungi, 8th edition,1995, CAB International, University Press, Cambridge, UK).

The fungal host cell may be a yeast cell. “Yeast” as used hereinincludes ascosporogenous yeast (Endomycetales), basidiosporogenousyeast, and yeast belonging to the Fungi Imperfecti (Blastomycetes).Since the classification of yeast may change in the future, for thepurposes of this invention, yeast shall be defined as described inBiology and Activities of Yeast (Skinner, Passmore, and Davenport,editors, Soc. App. Bacteriol. Symposium Series No. 9, 1980).

The yeast host cell may be a Candida, Hansenula, Kluyveromyces, Pichia,Saccharomyces, Schizosaccharomyces, or Yarrowia cell, such as aKluyveromyces lactis, Saccharomyces carlsbergensis, Saccharomycescerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii,Saccharomyces kluyveri, Saccharomyces norbensis, Saccharomycesoviformis, or Yarrowia lipolytica cell.

The fungal host cell may be a filamentous fungal cell. “Filamentousfungi” include all filamentous forms of the subdivision Eumycota andOomycota (as defined by Hawksworth et al., 1995, supra). The filamentousfungi are generally characterized by a mycelial wall composed of chitin,cellulose, glucan, chitosan, mannan, and other complex polysaccharides.Vegetative growth is by hyphal elongation and carbon catabolism isobligately aerobic. In contrast, vegetative growth by yeasts such asSaccharomyces cerevisiae is by budding of a unicellular thallus andcarbon catabolism may be fermentative.

The filamentous fungal host cell may be an Acremonium, Aspergillus,Aureobasidium, Bjerkandera, Ceriporiopsis, Chrysosporium, Coprinus,Coriolus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe,Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces,Penicillium, Phanerochaete, Phlebia, Piromyces, Pleurotus,Schizophyllum, Talaromyces, Thermoascus, Thielavia, Tolypocladium,Trametes, or Trichoderma cell.

For example, the filamentous fungal host cell may be an Aspergillusawamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillusjaponicus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae,Bjerkandera adusta, Ceriporiopsis aneirina, Ceriporiopsis caregiea,Ceriporiopsis gilvescens, Ceriporiopsis pannocinta, Ceriporiopsisrivulosa, Ceriporiopsis subrufa, Ceriporiopsis subvermispora,Chrysosporium inops, Chrysosporium keratinophilum, Chrysosporiumlucknowense, Chrysosporium merdarium, Chrysosporium pannicola,Chrysosporium queenslandicum, Chrysosporium tropicum, Chrysosporiumzonatum, Coprinus cinereus, Coriolus hirsutus, Fusarium bactridioides,Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusariumgraminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi,Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusariumsambucinum, Fusarium sarcochroum, Fusarium sporotrichioides, Fusariumsulphureum, Fusarium torulosum, Fusarium trichothecioides, Fusariumvenenatum, Humicola insolens, Humicola lanuginosa, Mucor miehei,Myceliophthora thermophila, Neurospora crassa, Penicillium purpurogenum,Phanerochaete chrysosporium, Phlebia radiata, Pleurotus eryngii,Thielavia terrestris, Trametes villosa, Trametes versicolor, Trichodermaharzianum, Trichoderma koningii, Trichoderma longibrachiatum,Trichoderma reesei, or Trichoderma viride cell.

Fungal cells may be transformed by a process involving protoplastformation, transformation of the protoplasts, and regeneration of thecell wall in a manner known per se. Suitable procedures fortransformation of Aspergillus and Trichoderma host cells are describedin EP 238023, Yelton et al., 1984, Proc. Natl. Acad. Sci. USA 81:1470-1474, and Christensen et al., 1988, Bio/Technology 6: 1419-1422.Suitable methods for transforming Fusarium species are described byMalardier et al., 1989, Gene 78: 147-156, and WO 96/00787. Yeast may betransformed using the procedures described by Becker and Guarente, InAbelson, J. N. and Simon, M. I., editors, Guide to Yeast Genetics andMolecular Biology, Methods in Enzymology, Volume 194, pp 182-187,Academic Press, Inc., New York; Ito et al., 1983, J. Bacteriol. 153:163; and Hinnen et al., 1978, Proc. Natl. Acad. Sci. USA 75: 1920.

Methods of Production

The present invention also relates to methods of producing a polypeptideof the present invention, comprising (a) cultivating a cell, which inits wild-type form produces the polypeptide, under conditions conducivefor production of the polypeptide; and (b) recovering the polypeptide.In a preferred aspect, the cell is a Paenibacillus cell, or aMicrobacterium cell.

The present invention also relates to methods of producing a polypeptideof the present invention, comprising (a) cultivating a recombinant hostcell of the present invention under conditions conducive for productionof the polypeptide; and (b) recovering the polypeptide.

The host cells are cultivated in a nutrient medium suitable forproduction of the polypeptide using methods known in the art. Forexample, the cell may be cultivated by shake flask cultivation, orsmall-scale or large-scale fermentation (including continuous, batch,fed-batch, or solid state fermentations) in laboratory or industrialfermentors performed in a suitable medium and under conditions allowingthe polypeptide to be expressed and/or isolated. The cultivation takesplace in a suitable nutrient medium comprising carbon and nitrogensources and inorganic salts, using procedures known in the art. Suitablemedia are available from commercial suppliers or may be preparedaccording to published compositions (e.g., in catalogues of the AmericanType Culture Collection). If the polypeptide is secreted into thenutrient medium, the polypeptide can be recovered directly from themedium. If the polypeptide is not secreted, it can be recovered fromcell lysates.

The polypeptide may be detected using methods known in the art that arespecific for the polypeptides such as methods for determining celluloseor xanthan lyase activity. These detection methods include, but are notlimited to, use of specific antibodies, formation of an enzyme product,or disappearance of an enzyme substrate. For example, an enzyme assaymay be used to determine the activity of the polypeptide.

The polypeptide may be recovered using methods known in the art. Forexample, the polypeptide may be recovered from the nutrient medium byconventional procedures including, but not limited to, collection,centrifugation, filtration, extraction, spray-drying, evaporation, orprecipitation.

The polypeptide may be purified by a variety of procedures known in theart including, but not limited to, chromatography (e.g., ion exchange,affinity, hydrophobic, chromatofocusing, and size exclusion),electrophoretic procedures (e.g., preparative isoelectric focusing),differential solubility (e.g., ammonium sulfate precipitation),SDS-PAGE, or extraction (see, e.g., Protein Purification, Janson andRyden, editors, VCH Publishers, New York, 1989) to obtain substantiallypure polypeptides.

In an alternative aspect, the polypeptide is not recovered, but rather ahost cell of the present invention expressing the polypeptide is used asa source of the polypeptide.

Fermentation Broth Formulations or Cell Compositions

The present invention also relates to a fermentation broth formulationor a cell composition comprising a polypeptide of the present invention.The fermentation broth product further comprises additional ingredientsused in the fermentation process, such as, for example, cells(including, the host cells containing the gene encoding the polypeptideof the present invention which are used to produce the polypeptide ofinterest), cell debris, biomass, fermentation media and/or fermentationproducts. In some embodiments, the composition is a cell-killed wholebroth containing organic acid(s), killed cells and/or cell debris, andculture medium.

The term “fermentation broth” as used herein refers to a preparationproduced by cellular fermentation that undergoes no or minimal recoveryand/or purification. For example, fermentation broths are produced whenmicrobial cultures are grown to saturation, incubated undercarbon-limiting conditions to allow protein synthesis (e.g., expressionof enzymes by host cells) and secretion into cell culture medium. Thefermentation broth can contain unfractionated or fractionated contentsof the fermentation materials derived at the end of the fermentation.Typically, the fermentation broth is unfractionated and comprises thespent culture medium and cell debris present after the microbial cells(e.g., filamentous fungal cells) are removed, e.g., by centrifugation.In some embodiments, the fermentation broth contains spent cell culturemedium, extracellular enzymes, and viable and/or nonviable microbialcells.

In an embodiment, the fermentation broth formulation and cellcompositions comprise a first organic acid component comprising at leastone 1-5 carbon organic acid and/or a salt thereof and a second organicacid component comprising at least one 6 or more carbon organic acidand/or a salt thereof. In a specific embodiment, the first organic acidcomponent is acetic acid, formic acid, propionic acid, a salt thereof,or a mixture of two or more of the foregoing and the second organic acidcomponent is benzoic acid, cyclohexanecarboxylic acid, 4-methylvalericacid, phenylacetic acid, a salt thereof, or a mixture of two or more ofthe foregoing.

In one aspect, the composition contains an organic acid(s), andoptionally further contains killed cells and/or cell debris. In oneembodiment, the killed cells and/or cell debris are removed from acell-killed whole broth to provide a composition that is free of thesecomponents.

The fermentation broth formulations or cell compositions may furthercomprise a preservative and/or anti-microbial (e.g., bacteriostatic)agent, including, but not limited to, sorbitol, sodium chloride,potassium sorbate, and others known in the art.

The cell-killed whole broth or composition may contain theunfractionated contents of the fermentation materials derived at the endof the fermentation. Typically, the cell-killed whole broth orcomposition contains the spent culture medium and cell debris presentafter the microbial cells (e.g., filamentous fungal cells) are grown tosaturation, incubated under carbon-limiting conditions to allow proteinsynthesis. In some embodiments, the cell-killed whole broth orcomposition contains the spent cell culture medium, extracellularenzymes, and killed filamentous fungal cells. In some embodiments, themicrobial cells present in the cell-killed whole broth or compositioncan be permeabilized and/or lysed using methods known in the art.

A whole broth or cell composition as described herein is typically aliquid, but may contain insoluble components, such as killed cells, celldebris, culture media components, and/or insoluble enzyme(s). In someembodiments, insoluble components may be removed to provide a clarifiedliquid composition.

The whole broth formulations and cell compositions of the presentinvention may be produced by a method described in WO 90/15861 or WO2010/096673.

Detergent Compositions

In one embodiment, the invention is directed to detergent compositionscomprising an enzyme of the present invention in combination with one ormore additional cleaning composition components. The choice ofadditional components is within the skill of the artisan and includesconventional ingredients, including the exemplary non-limitingcomponents set forth below.

The choice of components may include, for textile care, theconsideration of the type of textile to be cleaned, the type and/ordegree of soiling, the temperature at which cleaning is to take place,and the formulation of the detergent product. Although componentsmentioned below are categorized by general header according to aparticular functionality, this is not to be construed as a limitationsince the component may have one or more additional functionalitieswhich the skilled artisan will appreciate.

The detergent composition may be suitable for the laundering of textilessuch as e.g. fabrics, cloths or linen, or for cleaning hard surfacessuch as e.g. floors, tables, or dish wash.

Enzyme of the Present Invention

In one embodiment of the present invention, the a polypeptide of thepresent invention may be added to a detergent composition in an amountcorresponding to 0.0001-200 mg of enzyme protein, such as 0.0005-100 mgof enzyme protein, preferably 0.001-30 mg of enzyme protein, morepreferably 0.005-8 mg of enzyme protein, even more preferably 0.01-2 mgof enzyme protein per liter of wash liquor.

A composition for use in automatic dishwash (ADW), for example, mayinclude 0.0001%-50%, such as 0.001%-20%, such as 0.01%-10%, such as0.05-5% of enzyme protein by weight of the composition.

A composition for use in laundry granulation, for example, may include0.0001%-50%, such as 0.001%-20%, such as 0.01%-10%, such as 0.05%-5% ofenzyme protein by weight of the composition.

A composition for use in laundry liquid, for example, may include0.0001%-10%, such as 0.001-7%, such as 0.1%-5% of enzyme protein byweight of the composition.

The enzyme(s) of the detergent composition of the invention may bestabilized using conventional stabilizing agents, e.g., a polyol such aspropylene glycol or glycerol, a sugar or sugar alcohol, lactic acid,boric acid, or a boric acid derivative, e.g., an aromatic borate ester,or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid,and the composition may be formulated as described in, for example,WO92/19709 and WO92/19708.

In certain markets different wash conditions and, as such, differenttypes of detergents are used. This is disclosed in e.g. EP 1 025 240.For example, In Asia (Japan) a low detergent concentration system isused, while the United States uses a medium detergent concentrationsystem, and Europe uses a high detergent concentration system.

A low detergent concentration system includes detergents where less thanabout 800 ppm of detergent components are present in the wash water.Japanese detergents are typically considered low detergent concentrationsystem as they have approximately 667 ppm of detergent componentspresent in the wash water.

A medium detergent concentration includes detergents where between about800 ppm and about 2000 ppm of detergent components are present in thewash water. North American detergents are generally considered to bemedium detergent concentration systems as they have approximately 975ppm of detergent components present in the wash water.

A high detergent concentration system includes detergents where greaterthan about 2000 ppm of detergent components are present in the washwater. European detergents are generally considered to be high detergentconcentration systems as they have approximately 4500-5000 ppm ofdetergent components in the wash water.

Latin American detergents are generally high suds phosphate builderdetergents and the range of detergents used in Latin America can fall inboth the medium and high detergent concentrations as they range from1500 ppm to 6000 ppm of detergent components in the wash water. Suchdetergent compositions are all embodiments of the invention.

A polypeptide of the present invention may also be incorporated in thedetergent formulations disclosed in WO97/07202, which is herebyincorporated by reference.

Surfactants

The detergent composition may comprise one or more surfactants, whichmay be anionic and/or cationic and/or non-ionic and/or semi-polar and/orzwitterionic, or a mixture thereof. In a particular embodiment, thedetergent composition includes a mixture of one or more nonionicsurfactants and one or more anionic surfactants. The surfactant(s) istypically present at a level of from about 0.1% to 60% by weight, suchas about 1% to about 40%, or about 3% to about 20%, or about 3% to about10%. The surfactant(s) is chosen based on the desired cleaningapplication, and includes any conventional surfactant(s) known in theart. Any surfactant known in the art for use in detergents may beutilized.

When included therein the detergent will usually contain from about 1%to about 40% by weight, such as from about 5% to about 30%, includingfrom about 5% to about 15%, or from about 20% to about 25% of an anionicsurfactant. Non-limiting examples of anionic surfactants includesulfates and sulfonates, in particular, linear alkylbenzenesulfonates(LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS),phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates,alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonatesand disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate(SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS),alcohol ethersulfates (AES or AEOS or FES, also known as alcoholethoxysulfates or fatty alcohol ether sulfates), secondaryalkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates,sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methylesters (alpha-SFMe or SES) including methyl ester sulfonate (MES),alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid(DTSA), fatty acid derivatives of amino acids, diesters and monoestersof sulfo-succinic acid or soap, and combinations thereof.

When included therein the detergent will usually contain from about 0%to about 10% by weight of a cationic surfactant. Non-limiting examplesof cationic surfactants include alklydimethylethanolamine quat (ADMEAQ),cetyltrimethylammonium bromide (CTAB), dimethyldistearylammoniumchloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternaryammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, andcombinations thereof.

When included therein the detergent will usually contain from about 0.2%to about 40% by weight of a non-ionic surfactant, for example from about0.5% to about 30%, in particular from about 1% to about 20%, from about3% to about 10%, such as from about 3% to about 5%, or from about 8% toabout 12%. Non-limiting examples of non-ionic surfactants includealcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylatedfatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such asethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenolethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides(APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fattyacid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides(EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine(glucamides, GA, or fatty acid glucamide, FAGA), as well as productsavailable under the trade names SPAN and TWEEN, and combinationsthereof.

When included therein the detergent will usually contain from about 0%to about 10% by weight of a semipolar surfactant. Non-limiting examplesof semipolar surfactants include amine oxides (AO) such asalkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide andN-(tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, fatty acidalkanolamides and ethoxylated fatty acid alkanolamides, and combinationsthereof.

When included therein the detergent will usually contain from about 0%to about 10% by weight of a zwitterionic surfactant. Non-limitingexamples of zwitterionic surfactants include betaine,alkyldimethylbetaine, sulfobetaine, and combinations thereof.

Hydrotropes

A hydrotrope is a compound that solubilises hydrophobic compounds inaqueous solutions (or oppositely, polar substances in a non-polarenvironment). Typically, hydrotropes have both hydrophilic and ahydrophobic character (so-called amphiphilic properties as known fromsurfactants); however the molecular structure of hydrotropes generallydo not favor spontaneous self-aggregation, see e.g. review by Hodgdonand Kaler (2007), Current Opinion in Colloid & Interface Science 12:121-128. Hydrotropes do not display a critical concentration above whichself-aggregation occurs as found for surfactants and lipids formingmiceller, lamellar or other well defined meso-phases. Instead, manyhydrotropes show a continuous-type aggregation process where the sizesof aggregates grow as concentration increases. However, many hydrotropesalter the phase behavior, stability, and colloidal properties of systemscontaining substances of polar and non-polar character, includingmixtures of water, oil, surfactants, and polymers. Hydrotropes areclassically used across industries from pharma, personal care, food, totechnical applications. Use of hydrotropes in detergent compositionsallow for example more concentrated formulations of surfactants (as inthe process of compacting liquid detergents by removing water) withoutinducing undesired phenomena such as phase separation or high viscosity.

The detergent may contain 0-5% by weight, such as about 0.5 to about 5%,or about 3% to about 5%, of a hydrotrope. Any hydrotrope known in theart for use in detergents may be utilized. Non-limiting examples ofhydrotropes include sodium benzene sulfonate, sodium p-toluene sulfonate(STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS),sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers,sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodiumethylhexyl sulfate, and combinations thereof.

Builders and Co-Builders

The detergent composition may contain about 0-65% by weight, such asabout 5% to about 45% of a detergent builder or co-builder, or a mixturethereof. In a dish wash detergent, the level of builder is typically40-65%, particularly 50-65%. The builder and/or co-builder mayparticularly be a chelating agent that forms water-soluble complexeswith Ca and Mg. Any builder and/or co-builder known in the art for usein laundry detergents may be utilized. Non-limiting examples of buildersinclude zeolites, diphosphates (pyrophosphates), triphosphates such assodium triphosphate (STP or STPP), carbonates such as sodium carbonate,soluble silicates such as sodium metasilicate, layered silicates (e.g.,SKS-6 from Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA),diethanolamine (DEA, also known as iminodiethanol), triethanolamine(TEA, also known as 2,2′,2″-nitrilotriethanol), and carboxymethyl inulin(CMI), and combinations thereof.

The detergent composition may also contain 0-20% by weight, such asabout 5% to about 10%, of a detergent co-builder, or a mixture thereof.The detergent composition may include include a co-builder alone, or incombination with a builder, for example a zeolite builder. Non-limitingexamples of co-builders include homopolymers of polyacrylates orcopolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylicacid/maleic acid) (PAA/PMA). Further non-limiting examples includecitrate, chelators such as aminocarboxylates, aminopolycarboxylates andphosphonates, and alkyl- or alkenylsuccinic acid. Additional specificexamples include 2,2′,2″-nitrilotriacetic acid (NTA),ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaaceticacid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N′-disuccinicacid (EDDS), methylglycinediacetic acid (MGDA), glutamicacid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diphosphonic acid(HEDP), ethylenediaminetetra-(methylenephosphonic acid) (EDTMPA),diethylenetriaminepentakis(methylenephosphonic acid) (DTPMPA or DTMPA),N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoaceticacid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), asparticacid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA),N-(2-sulfomethyl)-aspartic acid (SMAS), N-(2-sulfoethyl)-aspartic acid(SEAS), N-(2-sulfomethyl)-glutamic acid (SMGL),N-(2-sulfoethyl)-glutamic acid (SEGL), N-methyliminodiacetic acid(MIDA), α-alanine-N,N-diacetic acid (α-ALDA), serine-N,N-diacetic acid(SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diaceticacid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilicacid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA) andsulfomethyl-N,N-diacetic acid (SMDA),N-(2-hydroxyethyl)ethylidenediamine-N,N′,N′-triacetate (HEDTA),diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonicacid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), andcombinations and salts thereof. Further exemplary builders and/orco-builders are described in, e.g., WO 09/102854, U.S. Pat. No.5,977,053

Bleaching Systems

The detergent may contain 0-50% by weight, such as about 0.1% to about25%, of a bleaching system. Any bleaching system known in the art foruse in laundry detergents may be utilized. Suitable bleaching systemcomponents include bleaching catalysts, photobleaches, bleachactivators, sources of hydrogen peroxide such as sodium percarbonate andsodium perborates, preformed peracids and mixtures thereof. Suitablepreformed peracids include, but are not limited to, peroxycarboxylicacids and salts, percarbonic acids and salts, perimidic acids and salts,peroxymonosulfuric acids and salts, for example, Oxone (R), and mixturesthereof. Non-limiting examples of bleaching systems includeperoxide-based bleaching systems, which may comprise, for example, aninorganic salt, including alkali metal salts such as sodium salts ofperborate (usually mono- or tetra-hydrate), percarbonate, persulfate,perphosphate, persilicate salts, in combination with a peracid-formingbleach activator. The term bleach activator is meant herein as acompound which reacts with peroxygen bleach like hydrogen peroxide toform a peracid. The peracid thus formed constitutes the activatedbleach. Suitable bleach activators to be used herein include thosebelonging to the class of esters amides, imides or anhydrides. Suitableexamples are tetracetylethylene diamine (TAED), sodium4-[(3,5,5-trimethylhexanoyl)oxy]benzene sulfonate (ISONOBS), diperoxydodecanoic acid, 4-(dodecanoyloxy)benzenesulfonate (LOBS),4-(decanoyloxy)benzenesulfonate, 4-(decanoyloxy)benzoate (DOBS),4-(nonanoyloxy)-benzenesulfonate (NOBS), and/or those disclosed inWO98/17767. A particular family of bleach activators of interest wasdisclosed in EP624154 and particularly preferred in that family isacetyl triethyl citrate (ATC). ATC or a short chain triglyceride liketriacetin has the advantage that it is environmental friendly as iteventually degrades into citric acid and alcohol. Furthermore acetyltriethyl citrate and triacetin has a good hydrolytical stability in theproduct upon storage and it is an efficient bleach activator. FinallyATC provides a good building capacity to the laundry additive.Alternatively, the bleaching system may comprise peroxyacids of, forexample, the amide, imide, or sulfone type. The bleaching system mayalso comprise peracids such as 6-(phthalimido)peroxyhexanoic acid (PAP).The bleaching system may also include a bleach catalyst. In someembodiments the bleach component may be an organic catalyst selectedfrom the group consisting of organic catalysts having the followingformulae:

(iii) and mixtures thereof; wherein each R¹ is independently a branchedalkyl group containing from 9 to 24 carbons or linear alkyl groupcontaining from 11 to 24 carbons, preferably each R¹ is independently abranched alkyl group containing from 9 to 18 carbons or linear alkylgroup containing from 11 to 18 carbons, more preferably each R¹ isindependently selected from the group consisting of 2-propylheptyl,2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, n-dodecyl, n-tetradecyl,n-hexadecyl, n-octadecyl, iso-nonyl, iso-decyl, iso-tridecyl andiso-pentadecyl. Other exemplary bleaching systems are described, e.g. inWO2007/087258, WO2007/087244, WO2007/087259 and WO2007/087242. Suitablephotobleaches may for example be sulfonated zinc phthalocyanine

Polymers

The detergent may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2%or 0.2-1% of a polymer. Any polymer known in the art for use indetergents may be utilized. The polymer may function as a co-builder asmentioned above, or may provide antiredeposition, fiber protection, soilrelease, dye transfer inhibition, grease cleaning and/or anti-foamingproperties. Some polymers may have more than one of the above-mentionedproperties and/or more than one of the below-mentioned motifs. Exemplarypolymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol)(PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) orpoly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine),carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA,poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers,hydrophobically modified CMC (HM-CMC) and silicones, copolymers ofterephthalic acid and oligomeric glycols, copolymers of poly(ethyleneterephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP,poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO)and polyvinylpyrrolidone-vinylimidazole (PVPVI). Further exemplarypolymers include sulfonated polycarboxylates, polyethylene oxide andpolypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate. Otherexemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of theabove-mentioned polymers are also contemplated.

Fabric Hueing Agents

The detergent compositions of the present invention may also includefabric hueing agents such as dyes or pigments, which when formulated indetergent compositions can deposit onto a fabric when said fabric iscontacted with a wash liquor comprising said detergent compositions andthus altering the tint of said fabric through absorption/reflection ofvisible light. Fluorescent whitening agents emit at least some visiblelight. In contrast, fabric hueing agents alter the tint of a surface asthey absorb at least a portion of the visible light spectrum. Suitablefabric hueing agents include dyes and dye-clay conjugates, and may alsoinclude pigments. Suitable dyes include small molecule dyes andpolymeric dyes. Suitable small molecule dyes include small molecule dyesselected from the group consisting of dyes falling into the Colour Index(C.I.) classifications of Direct Blue, Direct Red, Direct Violet, AcidBlue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, ormixtures thereof, for example as described in WO2005/03274,WO2005/03275, WO2005/03276 and EP1876226 (hereby incorporated byreference). The detergent composition preferably comprises from about0.00003 wt % to about 0.2 wt %, from about 0.00008 wt % to about 0.05 wt%, or even from about 0.0001 wt % to about 0.04 wt % fabric hueingagent. The composition may comprise from 0.0001 wt % to 0.2 wt % fabrichueing agent, this may be especially preferred when the composition isin the form of a unit dose pouch. Suitable hueing agents are alsodisclosed in, e.g. WO 2007/087257 and WO2007/087243.

Additional Enzymes

The detergent additive as well as the detergent composition may compriseone or more [additional] enzymes such as a protease, lipase, cutinase,an amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase,galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.

In general the properties of the selected enzyme(s) should be compatiblewith the selected detergent, (i.e., pH-optimum, compatibility with otherenzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) shouldbe present in effective amounts.

Cellulases:

Suitable cellulases include those of bacterial or fungal origin.Chemically modified or protein engineered mutants are included. Suitablecellulases include cellulases from the genera Bacillus, Pseudomonas,Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulasesproduced from Humicola insolens, Myceliophthora thermophila and Fusariumoxysporum disclosed in U.S. Pat. No. 4,435,307, U.S. Pat. No. 5,648,263,U.S. Pat. No. 5,691,178, U.S. Pat. No. 5,776,757 and WO 89/09259.

Especially suitable cellulases are the alkaline or neutral cellulaseshaving color care benefits. Examples of such cellulases are cellulasesdescribed in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO98/08940. Other examples are cellulase variants such as those describedin WO 94/07998, EP 0 531 315, U.S. Pat. No. 5,457,046, U.S. Pat. No.5,686,593, U.S. Pat. No. 5,763,254, WO 95/24471, WO 98/12307 andPCT/DK98/00299.

Example of cellulases exhibiting endo-beta-1,4-glucanase activity (EC3.2.1.4) are those having described in WO02/099091.

Other examples of cellulases include the family 45 cellulases describedin WO96/29397, and especially variants thereof having substitution,insertion and/or deletion at one or more of the positions correspondingto the following positions in SEQ ID NO: 8 of WO 02/099091: 2, 4, 7, 8,10, 13, 15, 19, 20, 21, 25, 26, 29, 32, 33, 34, 35, 37, 40, 42, 42a, 43,44, 48, 53, 54, 55, 58, 59, 63, 64, 65, 66, 67, 70, 72, 76, 79, 80, 82,84, 86, 88, 90, 91, 93, 95, 95d, 95h, 95j, 97, 100, 101, 102, 103, 113,114, 117, 119, 121, 133, 136, 137, 138, 139, 140a, 141, 143a, 145, 146,147, 150e, 150j, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160c,160e, 160k, 161, 162, 164, 165, 168, 170, 171, 172, 173, 175, 176, 178,181, 183, 184, 185, 186, 188, 191, 192, 195, 196, 200, and/or 20,preferably selected among P19A, G20K, Q44K, N48E, Q119H or Q146 R.

Commercially available cellulases include Celluzyme™, and Carezyme™(Novozymes A/S), Clazinase™, and Puradax HA™ (Genencor InternationalInc.), and KAC-500(B)™ (Kao Corporation).

Proteases:

The additional enzyme may be another protease or protease variant. Theprotease may be of animal, vegetable or microbial origin, includingchemically or genetically modified mutants. Microbial origin ispreferred. It may be an alkaline protease, such as a serine protease ora metalloprotease. A serine protease may for example be of the S1family, such as trypsin, or the S8 family such as subtilisin. Ametalloproteases protease may for example be a thermolysin from e.g.family M4, M5, M7 or M8.

The term “subtilases” refers to a sub-group of serine protease accordingto Siezen et al., Protein Engng. 4 (1991) 719-737 and Siezen et al.Protein Science 6 (1997) 501-523. Serine proteases are a subgroup ofproteases characterized by having a serine in the active site, whichforms a covalent adduct with the substrate. The subtilases may bedivided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitasefamily, the Proteinase K family, the Lantibiotic peptidase family, theKexin family and the Pyrolysin family. In one aspect of the inventionthe protease may be a subtilase, such as a subtilisin or a varianthereof. Further the subtilases (and the serine proteases) arecharacterised by having two active site amino acid residues apart fromthe serine, namely a histidine and an aspartic acid residue.

Examples of subtilisins are those derived from Bacillus such assubtilisin lentus, Bacillus lentus, subtilisin Novo, subtilisinCarlsberg, Bacillus licheniformis, subtilisin BPN′, subtilisin 309,subtilisin 147 and subtilisin 168 described in WO 89/06279 and proteasePD138 (WO 93/18140). Additional serine protease examples are describedin WO 98/020115, WO 01/44452, WO 01/58275, WO 01/58276, WO 03/006602 andWO 04/099401. An example of a subtilase variants may be those havingmutations in any of the positions: 3, 4, 9, 15, 27, 36, 68, 76, 87, 95,96, 97, 98, 99, 100, 101, 102, 103, 104, 106, 118, 120, 123, 128, 129,130, 160, 167, 170, 194, 195, 199, 205, 217, 218, 222, 232, 235, 236,245, 248, 252 and 274 using the BPN′ numbering. More preferred thesubtilase variants may comprise the mutations: S3T, V4I, S9R, A15T,K27R, *36D, V68A, N76D, N87S,R, *97E, A98S, S99G,D,A, S99AD, S101G,M,RS103A, V104I,Y,N, S106A, G118V,R, H120D,N, N123S, S128L, P129Q, S130A,G160D, Y167A, R1705, A194P, G195E, V199M, V205I, L217D, N218D, M222S,A232V, K235L, Q236H, Q245R, N252K, T274A (using BPN′ numbering). Afurther preferred protease is the alkaline protease from Bacillus lentusDSM 5483, as described for example in WO 95/23221, and variants thereofwhich are described in WO 92/21760, WO 95/23221, EP 1921147 and EP1921148.

Examples of trypsin-like proteases are trypsin (e.g. of porcine orbovine origin) and the Fusarium protease described in WO 89/06270 and WO94/25583. Examples of useful proteases are the variants described in WO92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially thevariants with substitutions in one or more of the following positions:27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218,222, 224, 235, and 274.

Examples of metalloproteases are the neutral metalloprotease asdescribed in WO 07/044993.

Preferred commercially available protease enzymes include Alcalase™,Coronase™, Duralase™, Durazym™, Esperase™, Everlase™, Kannase™,Liquanase™, Liquanase Ultra™, Ovozyme™, Polarzyme™, Primase™, Relase™,Savinase and Savinase Ultra™, (Novozymes A/S), Axapem™ (Gist-BrocasesN.V.), BLAP and BLAP X (Henkel AG & Co. KGaA), Excellase™, FN2™, FN3™,FN4™, Maxaca™, Maxapem™, Maxatase™, Properase™, Purafast™, Purafect™,Purafect OxP™, Purafect Prime™ and Puramax™ (Genencor int.).

Lipases and Cutinases:

Suitable lipases and cutinases include those of bacterial or fungalorigin. Chemically modified or protein engineered mutant enzymes areincluded. Examples include lipase from Thermomyces, e.g. from T.lanuginosus (previously named Humicola lanuginosa) as described inEP258068 and EP305216, cutinase from Humicola, e.g. H. insolens(WO96/13580), lipase from strains of Pseudomonas (some of these nowrenamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes(EP218272), P. cepacia (EP331376), P. sp. strain SD705 (WO95/06720 &WO96/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyceslipases (WO10/065455), cutinase from Magnaporthe grisea (WO10/107560),cutinase from Pseudomonas mendocina (U.S. Pat. No. 5,389,536), lipasefrom Thermobifida fusca (WO11/084412), Geobacillus stearothermophiluslipase (WO11/084417), lipase from Bacillus subtilis (WO11/084599), andlipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis(WO12/137147).

Further examples are lipases sometimes referred to as acyltransferasesor perhydrolases, e.g. acyltransferases with homology to Candidaantarctica lipase A (WO10/111143), acyltransferase from Mycobacteriumsmegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279),and variants of the M. smegmatis perhydrolase in particular the 554Vvariant used in the commercial product Gentle Power Bleach from HuntsmanTextile Effects Pte Ltd (WO10/100028).

Other examples are lipase variants such as those described in EP407225,WO92/05249, WO94/01541, WO94/25578, WO95/14783, WO95/30744, WO95/35381,WO95/22615, WO96/00292, WO97/04079, WO97/07202, WO00/34450, WO00/60063,WO01/92502, WO07/87508 and WO09/109500.

Preferred commercial lipase products include Lipolase™, Lipex™; Lipolex™and Lipoclean™ (Novozymes N/S), Lumafast (originally from Genencor) andLipomax (originally from Gist-Brocades).

Amylases

The amylase may be an alpha-amylase, a beta-amylase or a glucoamylaseand may be of bacterial or fungal origin. Chemically modified or proteinengineered mutants are included. Amylases include, for example,alpha-amylases obtained from Bacillus, e.g., a special strain ofBacillus licheniformis, described in more detail in GB 1,296,839.

Examples of amylases are those having SEQ ID NO: 3 in WO 95/10603 orvariants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferredvariants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQID NO: 4 of WO 99/019467, such as variants with substitutions in one ormore of the following positions: 15, 23, 105, 106, 124, 128, 133, 154,156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243,264, 304, 305, 391, 408, and 444 of SEQ ID NO: 3 in WO 95/10603.

Further amylases which can be used are amylases having SEQ ID NO: 6 inWO 02/010355 or variants thereof having 90% sequence identity to SEQ IDNO: 6. Preferred variants of SEQ ID NO: 6 are those having a deletion inpositions 181 and 182 and a substitution in position 193.

Other amylase examples are hybrid alpha-amylase comprising residues 1-33of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ IDNO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformisalpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having90% sequence identity thereof. Preferred variants of this hybridalpha-amylase are those having a substitution, a deletion or aninsertion in one of more of the following positions: G48, T49, G107,H156, A181, N190, M197, I201, A209 and Q264. Most preferred variants ofthe hybrid alpha-amylase comprising residues 1-33 of the alpha-amylasederived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO2006/066594 and residues 36-483 of SEQ ID NO: 4 are those having thesubstitutions:

M197T;

H156Y+A181T+N190F+A209V+Q264S; or

G48+T49+G107+H156+A181+N190+I201+A209+Q264.

Further amylase examples are amylases having SEQ ID NO: 6 in WO99/019467 or variants thereof having 90% sequence identity to SEQ ID NO:6. Preferred variants of SEQ ID NO: 6 are those having a substitution, adeletion or an insertion in one or more of the following positions:R181, G182, H183, G184, N195, I206, E212, E216 and K269. Particularlypreferred amylases are those having deletion in positions G182 and H183or positions H183 and G184.

Additional amylases are those having SEQ ID NO: 1, SEQ ID NO: 2 or SEQID NO: 7 of WO 96/023873 or variants thereof having 90% sequenceidentity to SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7. Preferredvariants of SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those havinga substitution, a deletion or an insertion in one or more of thefollowing positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260,269, 304 and 476. More preferred variants are those having a deletion inpositions 182 and 183 or positions 183 and 184. Most preferred amylasevariants of SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those havinga deletion in positions 183 and 184 and a substitution in positions 140,195, 206, 243, 260, 304 and 476.

Other amylases which can be used are amylases having SEQ ID NO: 2 of WO08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90%sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequenceidentity to SEQ ID NO: 10 in WO 01/66712. Preferred variants of SEQ IDNO: 10 in WO 01/66712 are those having a substitution, a deletion or aninsertion in one of more of the following positions: 176, 177, 178, 179,190, 201, 207, 211 and 264.

Further amylases which can be used are amylases having SEQ ID NO: 2 ofWO 09/061380 or variants thereof having 90% sequence identity to SEQ IDNO: 2. Preferred variants of SEQ ID NO: 2 are those having asubstitution, a deletion or an insertion in one of more of the followingpositions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182,G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359,K444 and G475. More preferred variants of SEQ ID NO: 2 are those havingthe substitution in one of more of the following positions: Q87E,R,Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E,R,N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/ordeletion in position R180 and/or S181. Most preferred amylase variantsof SEQ ID NO: 2 are those having the substitutions:

N128C+K178L+T182G+Y305R+G475K;

N128C+K178L+T182G+F202Y+Y305R+D319T+G475K;

S125A+N128C+K178L+T182G+Y305R+G475K; or

S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K wherein the variantoptionally further comprises a substitution at position 243 and/or adeletion at position 180 and/or position 181.

Other examples of amylases are the alpha-amylase having SEQ ID NO: 12 inWO01/66712 or a variant having at least 90%, such as at least 95%,sequence identity to SEQ ID NO: 12. Preferred amylase variants are thosehaving a substitution, a deletion or an insertion in one of more of thefollowing positions of SEQ ID NO: 12 in WO01/66712: R28, R118, N174;R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303,N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446,Q449, R458, N471, N484. Particular preferred amylases include variantshaving a deletion of D183 and G184 and having the substitutions R118K,N195F, R320K and R458K, and a variant additionally having substitutionsin one or more position selected from the group: M9, G149, G182, G186,M202, T257, Y295, N299, M323, E345 and A339, most preferred a variantthat additionally has substitutions in all these positions.

Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™,Stainzyme™, Stainzyme Plus™, Natalase™ and BAN™ (Novozymes A/S),Rapidase™ and Purastar™ (from Genencor International Inc.).

Peroxidases/Oxidases:

Suitable peroxidases/oxidases include those of plant, bacterial orfungal origin. Chemically modified or protein engineered mutants areincluded. Examples of useful peroxidases include peroxidases fromCoprinus, e.g., from C. cinereus, and variants thereof as thosedescribed in WO 93/24618, WO 95/10602, and WO 98/15257.

Commercially available peroxidases include Guardzyme™ (Novozymes N/S).

The detergent enzyme(s) may be included in a detergent composition byadding separate additives containing one or more enzymes, or by adding acombined additive comprising all of these enzymes. A detergent additiveof the invention, i.e., a separate additive or a combined additive, canbe formulated, for example, as a granulate, liquid, slurry, etc.Preferred detergent additive formulations are granulates, in particularnon-dusting granulates, liquids, in particular stabilized liquids, orslurries.

Non-dusting granulates may be produced, e.g., as disclosed in U.S. Pat.Nos. 4,106,991 and 4,661,452 and may optionally be coated by methodsknown in the art. Examples of waxy coating materials are poly(ethyleneoxide) products (polyethyleneglycol, PEG) with mean molar weights of1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethyleneoxide units; ethoxylated fatty alcohols in which the alcohol containsfrom 12 to 20 carbon atoms and in which there are 15 to 80 ethyleneoxide units; fatty alcohols; fatty acids; and mono- and di- andtriglycerides of fatty acids. Examples of film-forming coating materialssuitable for application by fluid bed techniques are given in GB1483591. Liquid enzyme preparations may, for instance, be stabilized byadding a polyol such as propylene glycol, a sugar or sugar alcohol,lactic acid or boric acid according to established methods. Protectedenzymes may be prepared according to the method disclosed in EP 238,216.

Adjunct Materials

Any detergent components known in the art for use in laundry detergentsmay also be utilized. Other optional detergent components includeanti-corrosion agents, anti-shrink agents, anti-soil redepositionagents, anti-wrinkling agents, bactericides, binders, corrosioninhibitors, disintegrants/disintegration agents, dyes, enzymestabilizers (including boric acid, borates, CMC, and/or polyols such aspropylene glycol), fabric conditioners including clays,fillers/processing aids, fluorescent whitening agents/opticalbrighteners, foam boosters, foam (suds) regulators, perfumes,soil-suspending agents, softeners, suds suppressors, tarnish inhibitors,and wicking agents, either alone or in combination. Any ingredient knownin the art for use in laundry detergents may be utilized. The choice ofsuch ingredients is well within the skill of the artisan.

Dispersants:

The detergent compositions of the present invention can also containdispersants. In particular powdered detergents may comprise dispersants.Suitable water-soluble organic materials include the homo- orco-polymeric acids or their salts, in which the polycarboxylic acidcomprises at least two carboxyl radicals separated from each other bynot more than two carbon atoms. Suitable dispersants are for exampledescribed in Powdered Detergents, Surfactant science series volume 71,Marcel Dekker, Inc.

Dye Transfer Inhibiting Agents:

The detergent compositions of the present invention may also include oneor more dye transfer inhibiting agents. Suitable polymeric dye transferinhibiting agents include, but are not limited to, polyvinylpyrrolidonepolymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidoneand N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles ormixtures thereof. When present in a subject composition, the dyetransfer inhibiting agents may be present at levels from about 0.0001%to about 10%, from about 0.01% to about 5% or even from about 0.1% toabout 3% by weight of the composition.

Fluorescent Whitening Agent:

The detergent compositions of the present invention will preferably alsocontain additional components that may tint articles being cleaned, suchas fluorescent whitening agent or optical brighteners. Where present thebrightener is preferably at a level of about 0.01% to about 0.5%. Anyfluorescent whitening agent suitable for use in a laundry detergentcomposition may be used in the composition of the present invention. Themost commonly used fluorescent whitening agents are those belonging tothe classes of diaminostilbene-sulphonic acid derivatives,diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.Examples of the diaminostilbene-sulphonic acid derivative type offluorescent whitening agents include the sodium salts of:4,4′-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino)stilbene-2,2′-disulphonate; 4,4′-bis-(2,4-dianilino-s-triazin-6-ylamino)stilbene-2,2′-disulphonate;4,4′-bis-(2-anilino-4(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino)stilbene-2,2′-disulphonate,4,4′-bis-(4-phenyl-2,1,3-triazol-2-yl)stilbene-2,2′-disulphonate;4,4′-bis-(2-anilino-4(1-methyl-2-hydroxy-ethylamino)-s-triazin-6-ylamino)stilbene-2,2′-disulphonate and2-(stilbyl-4″-naphtho-1,2′:4,5)-1,2,3-trizole-2″-sulphonate. Preferredfluorescent whitening agents are Tinopal DMS and Tinopal CBS availablefrom Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium saltof 4,4′-bis-(2-morpholino-4 anilino-s-triazin-6-ylamino) stilbenedisulphonate. Tinopal CBS is the disodium salt of2,2′-bis-(phenyl-styryl)disulphonate. Also preferred are fluorescentwhitening agents is the commercially available Parawhite KX, supplied byParamount Minerals and Chemicals, Mumbai, India. Other fluorescerssuitable for use in the invention include the 1-3-diaryl pyrazolines andthe 7-alkylaminocoumarins. Suitable fluorescent brightener levelsinclude lower levels of from about 0.01, from 0.05, from about 0.1 oreven from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt %.

Soil Release Polymers:

The detergent compositions of the present invention may also include oneor more soil release polymers which aid the removal of soils fromfabrics such as cotton and polyester based fabrics, in particular theremoval of hydrophobic soils from polyester based fabrics. The soilrelease polymers may for example be nonionic or anionic terephthalatebased polymers, polyvinyl caprolactam and related copolymers, vinylgraft copolymers, polyester polyamides see for example Chapter 7 inPowdered Detergents, Surfactant science series volume 71, Marcel Dekker,Inc. Another type of soil release polymers are amphiphilic alkoxylatedgrease cleaning polymers comprising a core structure and a plurality ofalkoxylate groups attached to that core structure. The core structuremay comprise a polyalkylenimine structure or a polyalkanolaminestructure as described in detail in WO 2009/087523 (hereby incorporatedby reference). Furthermore random graft co-polymers are suitable soilrelease polymers Suitable graft co-polymers are described in more detailin WO 2007/138054, WO 2006/108856 and WO 2006/113314 (herebyincorporated by reference). Other soil release polymers are substitutedpolysaccharide structures especially substituted cellulosic structuressuch as modified cellulose deriviatives such as those described in EP1867808 or WO 2003/040279 (both are hereby incorporated by reference).Suitable cellulosic polymers include cellulose, cellulose ethers,cellulose esters, cellulose amides and mixtures thereof. Suitablecellulosic polymers include anionically modified cellulose, nonionicallymodified cellulose, cationically modified cellulose, zwitterionicallymodified cellulose, and mixtures thereof. Suitable cellulosic polymersinclude methyl cellulose, carboxy methyl cellulose, ethyl cellulose,hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, estercarboxy methyl cellulose, and mixtures thereof.

Anti-Redeposition Agents:

The detergent compositions of the present invention may also include oneor more anti-redeposition agents such as carboxymethylcellulose (CMC),polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethyleneand/or polyethyleneglycol (PEG), homopolymers of acrylic acid,copolymers of acrylic acid and maleic acid, and ethoxylatedpolyethyleneimines. The cellulose based polymers described under soilrelease polymers above may also function as anti-redeposition agents.

Other suitable adjunct materials include, but are not limited to,anti-shrink agents, anti-wrinkling agents, bactericides, binders,carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foamregulators, hydrotropes, perfumes, pigments, sod suppressors, solvents,and structurants for liquid detergents and/or structure elasticizingagents.

Formulation of Detergent Products

The detergent composition of the invention may be in any convenientform, e.g., a bar, a homogenous tablet, a tablet having two or morelayers, a pouch having one or more compartments, a regular or compactpowder, a granule, a paste, a gel, or a regular, compact or concentratedliquid. There are a number of detergent formulation forms such as layers(same or different phases), pouches, as well as forms for machine dosingunit.

Pouches can be configured as single or multicompartments. It can be ofany form, shape and material which is suitable for hold the composition,e.g. without allowing the release of the composition from the pouchprior to water contact. The pouch is made from water soluble film whichencloses an inner volume. Said inner volume can be divided intocompartments of the pouch. Preferred films are polymeric materialspreferably polymers which are formed into a film or sheet. Preferredpolymers, copolymers or derivates thereof are selected polyacrylates,and water soluble acrylate copolymers, methyl cellulose, carboxy methylcellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose,hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, mostpreferably polyvinyl alcohol copolymers and, hydroxypropyl methylcellulose (HPMC). Preferably the level of polymer in the film forexample PVA is at least about 60%. Preferred average molecular weightwill typically be about 20,000 to about 150,000. Films can also be ofblend compositions comprising hydrolytically degradable and watersoluble polymer blends such as polyactide and polyvinyl alcohol (knownunder the Trade reference M8630 as sold by Chris Craft In. Prod. OfGary, Ind., US) plus plasticisers like glycerol, ethylene glycerol,Propylene glycol, sorbitol and mixtures thereof. The pouches cancomprise a solid laundry cleaning composition or part components and/ora liquid cleaning composition or part components separated by the watersoluble film. The compartment for liquid components can be different incomposition than compartments containing solids. Ref: (US2009/0011970A1).

Detergent ingredients can be separated physically from each other bycompartments in water dissolvable pouches or in different layers oftablets. Thereby negative storage interaction between components can beavoided. Different dissolution profiles of each of the compartments canalso give rise to delayed dissolution of selected components in the washsolution.

A liquid or gel detergent, which is not unit dosed, may be aqueous,typically containing at least 20% by weight and up to 95% water, such asup to about 70% water, up to about 65% water, up to about 55% water, upto about 45% water, up to about 35% water. Other types of liquids,including without limitation, alkanols, amines, diols, ethers andpolyols may be included in an aqueous liquid or gel. An aqueous liquidor gel detergent may contain from 0-30% organic solvent. A liquid or geldetergent may be non-aqueous.

Laundry Soap Bars

The enzymes of the invention may be added to laundry soap bars and usedfor hand washing laundry, fabrics and/or textiles. The term laundry soapbar includes laundry bars, soap bars, combo bars, syndet bars anddetergent bars. The types of bar usually differ in the type ofsurfactant they contain, and the term laundry soap bar includes thosecontaining soaps from fatty acids and/or synthetic soaps. The laundrysoap bar has a physical form which is solid and not a liquid, gel or apowder at room temperature. The term solid is defined as a physical formwhich does not significantly change over time, i.e. if a solid object(e.g. laundry soap bar) is placed inside a container, the solid objectdoes not change to fill the container it is placed in. The bar is asolid typically in bar form but can be in other solid shapes such asround or oval.

The laundry soap bar may contain one or more additional enzymes,protease inhibitors such as peptide aldehydes (or hydrosulfite adduct orhemiacetal adduct), boric acid, borate, borax and/or phenylboronic acidderivatives such as 4-formylphenylboronic acid, one or more soaps orsynthetic surfactants, polyols such as glycerine, pH controllingcompounds such as fatty acids, citric acid, acetic acid and/or formicacid, and/or a salt of a monovalent cation and an organic anion whereinthe monovalent cation may be for example Na⁺, K⁺ or NH₄ ⁺ and theorganic anion may be for example formate, acetate, citrate or lactatesuch that the salt of a monovalent cation and an organic anion may be,for example, sodium formate.

The laundry soap bar may also contain complexing agents like EDTA andHEDP, perfumes and/or different type of fillers, surfactants e.g.anionic synthetic surfactants, builders, polymeric soil release agents,detergent chelators, stabilizing agents, fillers, dyes, colorants, dyetransfer inhibitors, alkoxylated polycarbonates, suds suppressers,structurants, binders, leaching agents, bleaching activators, clay soilremoval agents, anti-redeposition agents, polymeric dispersing agents,brighteners, fabric softeners, perfumes and/or other compounds known inthe art.

The laundry soap bar may be processed in conventional laundry soap barmaking equipment such as but not limited to: mixers, plodders, e.g. atwo stage vacuum plodder, extruders, cutters, logo-stampers, coolingtunnels and wrappers. The invention is not limited to preparing thelaundry soap bars by any single method. The premix of the invention maybe added to the soap at different stages of the process. For example,the premix containing a soap, an enzyme, optionally one or moreadditional enzymes, a protease inhibitor, and a salt of a monovalentcation and an organic anion may be prepared and the mixture is thenplodded. The enzyme and optional additional enzymes may be added at thesame time as the protease inhibitor for example in liquid form. Besidesthe mixing step and the plodding step, the process may further comprisethe steps of milling, extruding, cutting, stamping, cooling and/orwrapping.

Granular Detergent Formulations

A granular detergent may be formulated as described in WO09/092699,EP1705241, EP1382668, WO07/001262, U.S. Pat. No. 6,472,364, WO04/074419or WO09/102854. Other useful detergent formulations are described inWO09/124162, WO09/124163, WO09/117340, WO09/117341, WO09/117342,WO09/072069, WO09/063355, WO09/132870, WO09/121757, WO09/112296,WO09/112298, WO09/103822, WO09/087033, WO09/050026, WO09/047125,WO09/047126, WO09/047127, WO09/047128, WO09/021784, WO09/010375,WO09/000605, WO09/122125, WO09/095645, WO09/040544, WO09/040545,WO09/024780, WO09/004295, WO09/004294, WO09/121725, WO09/115391,WO09/115392, WO09/074398, WO09/074403, WO09/068501, WO09/065770,WO09/021813, WO09/030632, and WO09/015951.

WO2011025615, WO2011016958, WO2011005803, WO2011005623, WO2011005730,WO2011005844, WO2011005904, WO2011005630, WO2011005830, WO2011005912,WO2011005905, WO2011005910, WO2011005813, WO2010135238, WO2010120863,WO2010108002, WO2010111365, WO2010108000, WO2010107635, WO2010090915,WO2010033976, WO2010033746, WO2010033747, WO2010033897, WO2010033979,WO2010030540, WO2010030541, WO2010030539, WO2010024467, WO2010024469,WO2010024470, WO2010025161, WO2010014395, WO2010044905,

WO2010145887, WO2010142503, WO2010122051, WO2010102861, WO2010099997,WO2010084039, WO2010076292, WO2010069742, WO2010069718, WO2010069957,WO2010057784, WO2010054986, WO2010018043, WO2010003783, WO2010003792,

WO2011023716, WO2010142539, WO2010118959, WO2010115813, WO2010105942,WO2010105961, WO2010105962, WO2010094356, WO2010084203, WO2010078979,WO2010072456, WO2010069905, WO2010076165, WO2010072603, WO2010066486,WO2010066631, WO2010066632, WO2010063689, WO2010060821, WO2010049187,WO2010031607, WO2010000636,

Method of Producing the Composition

The present invention also relates to methods of producing thecomposition. The method may be relevant for the (storage) stability ofthe detergent composition: e.g. Soap bar premix method WO2009155557.

Uses

The present invention is also directed to methods for using thecompositions thereof. Said invention may be used for example in anyapplication which requires the degradation of xanthan gum, such as indetergents and in the oil industry. In the oil industry xanthan gum isused for increasing the viscosity of the drilling fluid, in particularthe drilling mud. In all such uses there will also be the need todecrease the viscosity by degrading the xanthan gum, and for suchviscosity reduction a composition of the invention comprising a xanthanlyase and a GH 9 endoglucanase having activity on xanthan gum pretreatedwith xanthan lyase may suitable be used.

Use to Degrade Xanthan Gum

Xanthan gum has been use as an ingredient in many consumer productsincluding foods and cosmetics and has found use in the oil industry.Therefore the degradation of xanthan gum can result in improved cleaningprocesses, such as the easier removal of stains containing gums, such asxanthan gum, as well as the degradation of xanthan gum which is oftenused in the oil and drilling industry. Thus the present invention isdirected to the use of GH9 endoglucanases of the invention orcompositions thereof to degrade xanthan gum. The present invention isalso directed to the use of xanthan lyases of the invention orcompositions thereof to degrade xanthan gum. An embodiment is the use ofGH9 endoglucanases of the invention together with xanthan lyases of theinvention or compositions thereof to degrade xanthan gum. Degradation ofxanthan gum can preferably be measured using the viscosity reductionassay (ViPr assay) as described in example 6 or alternatively thereducing ends assay as described in Example 6 or the colourmetric assayas described in examples 25 and 26.

In an embodiment, degradation of xanthan gum may be measured using theviscosity reduction assay as described herein on xanthan gum. Apreferred embodiment is the use of xanthan gum (0.25% or 0.5%) in bufferor water wherein the drop in viscosity is measured after 5 minutes, 30minutes, 1 hour, 1.5 hours, 2 hours, 2.5 hours, 3 hours, 3.5 hours or 4hours. A more preferred embodiment is the use of xanthan gum (0.25%) inwater wherein the drop in viscosity is measured after 3 hours. Thepreferred enzyme concentration used for the GH9 endoglucanase andxanthan lyase is 31.25 mg EP/L and 31.25 mg EP/L respectively.

The drop in viscosity for the degradation of xanthan gum is at least 200Pa when using the viscosity reduction assay. The drop in viscosity forthe degradation of xanthan gum is at least 250 Pa when using theviscosity reduction assay. The drop in viscosity for the degradation ofxanthan gum is at least 300 Pa when using the viscosity reduction assay.The drop in viscosity for the degradation of xanthan gum is at least 350Pa when using the viscosity reduction assay. The drop in viscosity forthe degradation of xanthan gum is at least 400 Pa when using theviscosity reduction assay. The drop in viscosity for the degradation ofxanthan gum is at least 450 Pa when using the viscosity reduction assay.The drop in viscosity for the degradation of xanthan gum is at least 500Pa when using the viscosity reduction assay. The drop in viscosity forthe degradation of xanthan gum is at least 550 Pa when using theviscosity reduction assay. The drop in viscosity for the degradation ofxanthan gum is at least 600 Pa when using the viscosity reduction assay.

GH9 endoglucanase activity may alternatively be measured reducing endson xanthan gum pre-treated with xanthan lyase using the colorimetricassay developed by Lever (1972), Anal. Biochem. 47: 273-279, 1972. Apreferred embodiment is the use of 0.1% xanthan gum pre-treated withxanthan lyase. Degradation of xanthan gum pre-treated with xanthan lyasemay be determined by calculating difference between blank and samplewherein a difference of more than 0.5 mAU, preferably more than 0.6 mAU,more preferably more than 0.7 mAU or even more preferably more than 0.8mAU shows degradation of xanthan gum pre-treated with xanthan lyase.

Xanthan lyase activity may alternatively be measured reducing ends onxanthan gum using the colorimetric assay developed by Lever (1972),Anal. Biochem. 47: 273-279, 1972. A preferred embodiment is the use of0.1% xanthan gum. Degradation of xanthan gum may be determined bycalculating difference between blank and sample wherein a difference ofmore than 0.1 mAU, preferably more than 0.15 mAU, more preferably morethan 0.2 mAU or even more preferably more than 0.25 mAU showsdegradation of xanthan gum.

GH9 endoglucanase and xanthan lyase activity may alternatively bemeasured reducing ends on xanthan gum using the colorimetric assaydeveloped by Lever (1972), Anal. Biochem. 47: 273-279, 1972. A preferredembodiment is the use of 0.1% xanthan gum. Degradation of xanthan gummay be determined by calculating difference between blank and samplewherein a difference of more than 0.4 mAU, preferably more than 0.5 mAU,more preferably more than 0.6 mAU or even more preferably more than 0.8mAU shows degradation of xanthan gum. The invention also relates tomethods for degrading xanthan gum comprising applying a compositioncomprising one or more GH9 endoglucanases of the invention to xanthangum. The invention further relates to methods for degrading xanthan gumcomprising applying a composition comprising one or more xanthan lyasesof the invention to xanthan gum. An embodiment is a method for degradingxanthan gum comprising applying a composition comprising one or more GH9endoglucanases of the invention together with one or more xanthan lyasesof the invention to xanthan gum.

Use in Detergents.

The present invention is directed to the use of GH9 endoglucanases ofthe invention or compositions thereof in cleaning processes such as thelaundering of textiles and fabrics (e.g. household laundry washing andindustrial laundry washing), as well as household and industrial hardsurface cleaning, such as dish wash. The GH9 endoglucanases of theinvention may be added to a detergent composition comprising of one ormore detergent components.

The present invention is also directed to the use of xanthan lyases ofthe invention or compositions thereof in cleaning processes such as thelaundering of textiles and fabrics (e.g. household laundry washing andindustrial laundry washing), as well as household and industrial hardsurface cleaning, such as dish wash. The xanthan lyases of the inventionmay be added to a detergent composition comprising of one or moredetergent components.

An embodiment is the use of GH9 endoglucanases of the invention togetherwith xanthan lyases of the invention or compositions thereof in cleaningprocesses such as the laundering of textiles and fabrics (e.g. householdlaundry washing and industrial laundry washing), as well as householdand industrial hard surface cleaning, such as dish wash. The GH9endoglucanases of the invention together with xanthan lyases of theinvention may be added to a detergent composition comprising of one ormore detergent components.

The polypeptides of the present invention may be added to and thusbecome a component of a detergent composition. The detergent compositionof the present invention may be formulated, for example, as a hand ormachine laundry detergent composition for both household and industriallaundry cleaning, including a laundry additive composition suitable forpre-treatment of stained fabrics and a rinse added fabric softenercomposition, or be formulated as a detergent composition for use ingeneral household or industrial hard surface cleaning operations, or beformulated for hand or machine (both household and industrial)dishwashing operations. In a specific aspect, the present inventionprovides a detergent additive comprising a polypeptide of the presentinvention as described herein.

In an embodiment, the ΔInt enzyme value may be measured using the AMSAas described herein on xanthan gum with carbon black swatches. Apreferred embodiment is the use of xanthan gum with carbon black (DN31,DN31C or DN31D) swatches at 20° C. or at 40° C. A more preferredembodiment is the use of xanthan gum with carbon black (DN31C or DN31D)swatches at 40° C. An even more preferred embodiment is the use ofxanthan gum with carbon black (DN31D) swatches at 40° C. The preferredenzyme concentration used for the GH9 endoglucanase and xanthan lyase is0.5 mg EP/L and 1.0 mg EP/L respectively.

The delta intensity value for xanthan gum with carbon black swatch is atleast 3 units as determined by AMSA. The delta intensity value forxanthan gum with carbon black swatch is at least 3.5 units as determinedby AMSA. The delta intensity value for xanthan gum with carbon blackswatch is at least 4 units as determined by AMSA. The delta intensityvalue for xanthan gum with carbon black swatch is at least 4.5 units asdetermined by AMSA. The delta intensity value for xanthan gum withcarbon black swatch is at least 5 units as determined by AMSA. The deltaintensity value for xanthan gum with carbon black swatch is at least 5.5units as determined by AMSA. The delta intensity value for xanthan gumwith carbon black swatch is at least 6 units as determined by AMSA. Thedelta intensity value for xanthan gum with carbon black swatch is atleast 7 units as determined by AMSA. The delta intensity value forxanthan gum with carbon black swatch is at least 8 units as determinedby AMSA. The delta intensity value for xanthan gum with carbon blackswatch is at least 9 units as determined by AMSA. The delta intensityvalue for xanthan gum with carbon black swatch is at least 10 units asdetermined by AMSA.

In an embodiment, the ARem enzyme value may be measured using theMiniLOM assay as described herein on xanthan gum with carbon blackswatches. A preferred embodiment is the use of xanthan gum with carbonblack (DN31, DN31C or DN31D) swatches at 20° C. or at 40° C. A morepreferred embodiment is the use of xanthan gum with carbon black (DN31Cor DN31D) swatches at 40° C. An even more preferred embodiment is theuse of xanthan gum with carbon black (DN31D) swatches at 40° C. Theremission value is preferably measured at 460 nm. The preferred enzymeconcentration used for the GH9 endoglucanase and xanthan lyase is 0.5 mgEP/L and 1.0 mg EP/L respectively.

The ΔRem enzyme value for xanthan gum with carbon black swatch is atleast 1.5 units as determined by MiniLOM. The ΔRem enzyme value forxanthan gum with carbon black swatch is at least 1.75 units asdetermined by MiniLOM. The ΔRem enzyme value for xanthan gum with carbonblack swatch is at least 2 units as determined by MiniLOM. The ΔRemenzyme value for xanthan gum with carbon black swatch is at least 2.25units as determined by MiniLOM. The ΔRem enzyme value for xanthan gumwith carbon black swatch is at least 2.5 units as determined by MiniLOM.The ΔRem enzyme value for xanthan gum with carbon black swatch is atleast 2.75 units as determined by MiniLOM. The ΔRem enzyme value forxanthan gum with carbon black swatch is at least 3 units as determinedby MiniLOM. The ΔRem enzyme value for xanthan gum with carbon blackswatch is at least 3.5 units as determined by MiniLOM. The ΔRem enzymevalue for xanthan gum with carbon black swatch is at least 4 units asdetermined by MiniLOM. The ΔRem enzyme value for xanthan gum with carbonblack swatch is at least 4.5 units as determined by MiniLOM. The ΔRemenzyme value for xanthan gum with carbon black swatch is at least 5units as determined by MiniLOM.

The invention also relates to methods for degrading xanthan gum on thesurface of a textile or hard surface, such as dish wash, comprisingapplying a composition comprising one or more GH9 endoglucanases of theinvention to xanthan gum. The invention further relates to methods fordegrading xanthan gum on the surface of a textile or hard surface, suchas dish wash, comprising applying a composition comprising one or morexanthan lyases of the invention to xanthan gum. An embodiment is amethod for degrading xanthan gum on the surface of a textile or hardsurface, such as dish wash, comprising applying a composition comprisingone or more GH9 endoglucanases of the invention together with one ormore xanthan lyases of the invention to xanthan gum. An embodiment isthe composition comprising one or more detergent components as describedherein. Use of GH9 endoglucanases having an enzyme detergency benefit

It has surprisingly been found that the use of a GH9 alone gives anenzyme detergency benefit, preferably an enzyme detergency benefit onxanthan gum. This is surprising since endoglucanases are unable tosignificantly degrade the backbone of xanthan gum unless the xanthan gumhas been pre-treated with xanthan lyase.

Thus another aspect of the invention is the use of a detergentcomposition comprising one or more detergent components and an isolatedGH9 endoglucanase having an enzyme detergency benefit selected from thegroup consisting of

-   -   (a) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        2;    -   (b) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        10;    -   (c) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        12;    -   (d) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        14;    -   (e) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        48;    -   (f) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        52;    -   (g) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        56;    -   (h) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        82;    -   (i) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        86;    -   (j) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        90;    -   (k) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        94;    -   (l) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        98;    -   (m) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        102;    -   (n) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        130;    -   (o) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        134;    -   (p) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        138;    -   (q) a polypeptide encoded by a polynucleotide that hybridizes        under medium stringency conditions, medium-high stringency        conditions, high stringency conditions, or very high stringency        conditions with:        -   (i) the mature polypeptide coding sequence of SEQ ID NO: 1;        -   (ii) the mature polypeptide coding sequence of SEQ ID NO: 9;        -   (iii) the mature polypeptide coding sequence of SEQ ID NO:            11;        -   (iv) the mature polypeptide coding sequence of SEQ ID NO:            13;        -   (v) the mature polypeptide coding sequence of SEQ ID NO: 47;        -   (vi) the mature polypeptide coding sequence of SEQ ID NO:            51;        -   (vii) the mature polypeptide coding sequence of SEQ ID NO:            55;        -   (viii) the mature polypeptide coding sequence of SEQ ID NO:            81;        -   (ix) the mature polypeptide coding sequence of SEQ ID NO:            85;        -   (x) the mature polypeptide coding sequence of SEQ ID NO: 89;        -   (xi) the mature polypeptide coding sequence of SEQ ID NO:            93;        -   (xii) the mature polypeptide coding sequence of SEQ ID NO:            97;        -   (xiii) the mature polypeptide coding sequence of SEQ ID NO:            101;        -   (xiv) the mature polypeptide coding sequence of SEQ ID NO:            129;        -   (xv) the mature polypeptide coding sequence of SEQ ID NO:            133;        -   (xvi) the mature polypeptide coding sequence of SEQ ID NO:            137; or        -   (xvii) the full-length complement thereof of (i), (ii),            (iii), (iv), (v), (vi), (vii), (viii), (ix), (x), (xi),            (xii), (xiii), (xiv), (xv), or (xvi);    -   (r) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 1;    -   (s) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 9;    -   (t) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 11;    -   (u) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 13;    -   (v) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 47;    -   (w) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 51;    -   (x) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 55;    -   (y) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 81;    -   (z) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 85;    -   (aa) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 89;    -   (ab) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 93;    -   (ac) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 97;    -   (ad) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 101;    -   (ae) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 129;    -   (af) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 133;    -   (ag) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 137;    -   (ah) a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID        NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 48, SEQ ID NO:        52, SEQ ID NO: 56, SEQ ID NO: 82, SEQ ID NO: 86, SEQ ID NO: 90,        SEQ ID NO: 94, SEQ ID NO: 98, SEQ ID NO: 102, SEQ ID NO: 130,        SEQ ID NO: 134 or SEQ ID NO: 138 comprising a substitution,        deletion, and/or insertion at one or more positions (e.g.        several); and    -   (ai) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q), (r),        (s), (t), (u), (v), (w), (x), (y), (z), (aa), (ab), (ac), (ad),        (ae), (af), (ag) or (ah) that has activity on xanthan gum        pretreated with xanthan lyase.

An embodiment is the use of a detergent composition comprising one ormore detergent components and an isolated GH9 endoglucanase having anenzyme detergency benefit selected from the group consisting of

-   -   (a) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        2;    -   (b) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        10;    -   (c) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        14;    -   (d) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        48;    -   (e) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        52;    -   (f) a polypeptide having at least 80%, e.g., at least 81%, at        least 82%, at least 83%, at least 84%, at least 85%, at least        86%, at least 87%, at least 88%, at least 89%, at least 90%, at        least 91%, at least 92%, at least 93%, at least 94%, at least        95%, at least 96%, at least 97%, at least 98%, at least 99%, or        100% sequence identity to the mature polypeptide of SEQ ID NO:        56;    -   (g) a polypeptide encoded by a polynucleotide that hybridizes        under medium stringency conditions, medium-high stringency        conditions, high stringency conditions, or very high stringency        conditions with:        -   (i) the mature polypeptide coding sequence of SEQ ID NO: 1;        -   (ii) the mature polypeptide coding sequence of SEQ ID NO: 9;        -   (iii) the mature polypeptide coding sequence of SEQ ID NO:            13;        -   (iv) the mature polypeptide coding sequence of SEQ ID NO:            47;        -   (v) the mature polypeptide coding sequence of SEQ ID NO: 51;        -   (vi) the mature polypeptide coding sequence of SEQ ID NO:            55;        -   (vii) the full-length complement thereof of (i), (ii),            (iii), (iv), (v) or (vi);    -   (h) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 1;    -   (i) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 9;    -   (j) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 13;    -   (k) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 47;    -   (l) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 51;    -   (m) a polypeptide encoded by a polynucleotide having at least        80%, e.g., at least 81%, at least 82%, at least 83%, at least        84%, at least 85%, at least 86%, at least 87%, at least 88%, at        least 89%, at least 90%, at least 91%, at least 92%, at least        93%, at least 94%, at least 95%, at least 96%, at least 97%, at        least 98%, at least 99%, or 100% sequence identity to the mature        polypeptide coding sequence of SEQ ID NO: 55;    -   (n) a variant of the mature polypeptide of SEQ ID NO: 2, SEQ ID        NO: 10, SEQ ID NO: 14, SEQ ID NO: 48, SEQ ID NO: 52 or SEQ ID        NO: 56 comprising a substitution, deletion, and/or insertion at        one or more positions (e.g. several); and    -   (o) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m) or (n) that has activity        on xanthan gum pretreated with xanthan lyase.

Another embodiment is the use of a detergent composition comprising oneor more detergent components and an isolated GH9 endoglucanase of theinvention together with a xanthan lyase. A preferred embodiment is theuse of a detergent composition comprising one or more detergentcomponents and an isolated GH9 endoglucanase of the invention togetherwith a xanthan lyase of the invention.

Use in the Fracturing of a Subterranean Formation (Oil Drilling)

Hydraulic fracturing is used to create subterranean fractures thatextend from the borehole into rock formation in order to increase therate at which fluids can be produced by the formation. Generally, a highviscosity fracturing fluid is pumped into the well at sufficientpressure to fracture the subterranean formation. In order to maintainthe increased exposure to the formation, a solid proppant is added tothe fracturing fluid which is carried into the fracture by the highpressure applied to the fluid. Once the high viscosity fracturing fluidhas carried the proppant into the formation, breakers are used to reducethe fluid's viscosity which allows the proppant to settle into thefracture and thereby increase the exposure of the formation to the well.Breakers work by reducing the molecular weight of the polymers, thus‘breaking’ or degrading the polymer. The fracture then becomes a highpermeability conduit for fluids and gas to be produced back to the well.Such processes are further disclosed in U.S. Pat. Nos. 7,360,593,5,806,597, 5,562,160, 5,201,370 and 5,067,566.

Thus the invention relates to the use of GH9 endoglucanases of theinvention as enzyme breakers. The invention also relates to the use ofxanthan lyases of the invention as enzyme breakers. An embodiment of theinvention is the use of GH9 endoglucanases of the invention togetherwith xanthan lyases of the invention as enzyme breakers.

Accordingly, the invention provides a method for breaking xanthan gum ina well bore comprising: (i) blending together a gellable fracturingfluid comprising aqueous fluid, one or more hydratable polymers,suitable cross-linking agents for cross-linking the hydratable polymerto form a polymer gel and one or more enzymes of the invention (i.e. theenzyme breaker); (ii) pumping the cross-linked polymer gel into the wellbore under sufficient pressure to fracture the surrounding formation;and (iii) allowing the enzyme breaker to degrade the cross-linkedpolymer to reduce the viscosity of the fluid so that the fluid can bepumped from the formation back to the well surface. As such, the GH9endoglucanases of the invention can be used to control the viscosity offracturing fluids. Furthermore, the xanthan lyases of the invention canbe used to control the viscosity of fracturing fluids. In an embodiment,one or more GH9 endoglucanases of the invention together with one ormore xanthan lyases of the invention can be used to control theviscosity of fracturing fluids.

The enzyme breaker of the present invention may be an ingredient of afracturing fluid or a breaker-crosslinker-polymer complex which furthercomprises a hydratable polymer and a crosslinking agent. The fracturingfluid or complex may be a gel or may be gellable. The complex is usefulin a method for using the complex in a fracturing fluid to fracture asubterranean formation that surrounds a well bore by pumping the fluidto a desired location within the well bore under sufficient pressure tofracture the surrounding subterranean formation. The complex may bemaintained in a substantially non-reactive state by maintaining specificconditions of pH and temperature, until a time at which the fluid is inplace in the well bore and the desired fracture is completed. Once thefracture is completed, the specific conditions at which the complex isinactive are no longer maintained. When the conditions changesufficiently, the complex becomes active and the breaker begins tocatalyze polymer degradation causing the fracturing fluid to becomesufficiently fluid to be pumped from the subterranean formation to thewell surface.

Other Uses

The polypeptides of the present invention may additionally be used inother application where it is beneficial to remove xanthan gum.

Methods

Method of Degrading Xanthan Gum Wherein the Xanthan Gum is Used inFracturing of a Subterranean Formation Perpetrated by a Well Bore

When a well is drilled, reservoir drilling fluid (RDF) is circulatedwithin the drilling equipment to cool down and clean the drill bit,remove the drill cuttings out of the well bore, reduce friction betweenthe drill string and the sides of the borehole, and form a filtercake inorder to prevent fluid leak off into the formation. The driving forcefor the formation of the filtercake is the higher wellbore pressureapplied to maintain the borehole stability. This filtercake restrictsthe inflow of reservoir fluids into the wellbore during the drillingprocess and placement of the completion. If the filtercake damage thatis created during the drilling process is not removed prior to or duringcompletion of the well, a range of issues can arise when the well is puton production, i.e., completion equipment failures and impairedreservoir productivity.

Drilling fluid (mud), also called reservoir drilling fluid (RDF), can besynthetic/oil based or water based. To minimize invasion of the drillingfluid into the formation, both oil based and water based mud filtercakestypically contain a bridging or weighting agent, usually particles ofcalcium carbonate, barite or a mixture of the two, that bridge at thepore throats of the formation and thereby form a relatively lowpermeability filtercake. Both oil based and water based mud filtercakesalso contain solids called cuttings that have been picked up duringdrilling, as opposed to the bridging/weighting agents that are added inthe formulation of the drilling fluid. These solids can be quartz(sand), silts and/or shales, depending on the reservoir formation aswell as the formations traversed by the drilling path to the reservoir.In addition, oil based drilling muds contain water droplets that becometrapped in the pore space of the filtercake, while water based mudfiltercakes contain polymers, such as starch and xanthan gum, and otherinorganic salts.

The formation of a mud filtercake is often necessary for drilling,particularly in unconsolidated formations with wellbore stabilityproblems and typically high permeabilities. The filtercake is thentreated with various chemicals, such as chelants or acids to dissolvethe calcite component; and/or enzymes or oxidizers to degrade thepolymer component to recover permeability.

In one aspect, the invention provides a method for degrading xanthan gumwherein xanthan gum is used in fracturing of a subterranean formationperpetrated by a well bore by applying a composition comprising one ofmore enzymes of the invention. The method can include the steps of: (i)pumping a treatment fluid comprising one or more enzymes of theinvention into the borehole in contact with the filtercake to be removedto establish a differential pressure between the treatment fluid and theformation adjacent the filtercake and (ii) evenly propagating treatmentof the filtercake during the differential pressure period to delaybreakthrough by the treatment fluid.

In one embodiment, the method can include establishing permeabilitythrough the treated filtercake between the formation and the borehole.In another embodiment, the filtercake can include drilling solids andclays, and may be formed from an aqueous drilling fluid. If desired, thetreatment fluid for treating the aqueous drilling fluid filtercake canalso include an oxidizer and/or a chelant, or it can be substantiallyfree of chelant and oxidizer additives. In another example, thefiltercake can be formed from an oil or invert emulsion drilling fluid.If desired, the treatment fluid for treating the oil or invert emulsiondrilling fluid filtercake can also include a mutual solvent, awater-wetting agent or a combination thereof to disperse hydrophobiccomponents in the filtercake.

In one embodiment, the treatment fluid comprises one or more GH9endoglucanases of the invention. In another embodiment, the treatmentfluid comprises one or more xanthan lyases of the invention. In apreferred embodiment, the treatment fluid comprises one or more GH9endoglucanases and one or more xanthan lyases of the invention.

Method of Degrading Xanthan Gum Wherein the Xanthan Gum is a Componentin Borehole Filtercake

In one aspect, the invention provides a method for cleaning boreholefiltercake, comprising polymers, such as xanthan gum and drilling fluidsolids once the filtercake has been pumped to the surface. Drilling mudis pumped from mud pits to the drill bit and then back out to thesurface, carrying out amongst other things crushed or cut rock(cuttings) in the process. The cuttings are filtered out and the mud isreturned to the mud pits where fines can settle and/or chemicals orenzymes (breakers) can be added.

The method for degrading xanthan gum wherein the xanthan gum is acomponent in borehole filtercake can include the steps of (i) treatingthe borehole filtercake with a treatment fluid comprising one or moreenzymes of the invention and (ii) separating the solids from the fluids.In one embodiment, the treatment fluid comprises one or more GH9endoglucanases of the invention. In another embodiment, the treatmentfluid comprises one or more xanthan lyases of the invention. In apreferred embodiment, the treatment fluid comprises one or more GH9endoglucanases of the invention and one or more xanthan lyases of theinvention.

The borehole filtercake may be treated in mud pits with one or moreenzymes of the invention and the drilling fluid can be re-circulated.Alternatively, once the filtercake has been treated with one or moreenzymes of the invention, the solids and fluid are separated usingsolid-liquid separation processes, such as centrifugation.

The present invention is further described by the following examplesthat should not be construed as limiting the scope of the invention.

EXAMPLES

Media and Solutions

YP+2% glucose medium was composed of 1% yeast extract, 2% peptone and 2%glucose.

PDA agar plates were composed of potato infusion (potato infusion wasmade by boiling 300 g of sliced (washed but unpeeled) potatoes in waterfor 30 minutes and then decanting or straining the broth throughcheesecloth. Distilled water was then added until the total volume ofthe suspension was one liter, followed by 20 g of dextrose and 20 g ofagar powder. The medium was sterilized by autoclaving at 15 psi for 15minutes (Bacteriological Analytical Manual, 8th Edition, Revision A,1998).

LB plates were composed of 10 g of Bacto-Tryptone, 5 g of yeast extract,10 g of sodium chloride, 15 g of Bacto-agar, and deionized water to 1liter. The medium was sterilized by autoclaving at 15 psi for 15 minutes(Bacteriological Analytical Manual, 8th Edition, Revision A, 1998).

COVE sucrose plates were composed of 342 g Sucrose (Sigma S-9378), 20 gAgar powder, 20 ml Cove salt solution (26 g MgSO₄.7H₂O, 26 g KCL, 26 gKH₂PO₄, 50 ml Cove trace metal solution) and deionized water to 1liter), and deionized water to 1 liter). The medium was sterilized byautoclaving at 15 psi for 15 minutes (Bacteriological Analytical Manual,8th Edition, Revision A, 1998). The medium was cooled to 60° C. andadded 10 mM acetamide, 15 mM CsCl, Triton X-100 (50 μl/500 ml)).

Cove trace metal solution was composed of 0.04 g Na₂B₄O₇.10H₂O, 0.4 gCuSO₄.5H₂O, 1.2 g FeSO₄.7H₂O, 0.7 g MnSO₄.H₂O, 0.8 g Na₂MoO₄.2H₂O, 10 gZnSO₄.7H₂O, and deionized water to 1 liter.

Dap-4C medium was composed of 20 g Dextrose, 10 g Maltose, 11 gMgSO₄.7H₂O, 1 g KH₂PO₄, 2 g Citric Acid, 5.2 g K₃PO₄.H₂O, 0.5 g YeastExtract (Difco), 1 ml Dowfax 63N10 (Dow Chemical Company), 0.5 ml KU6trace metals solution, 2.5 g CaCO₃, and deionized water to 1 liter. Themedium was sterilized by autoclaving at 15 psi for 15 minutes(Bacteriological Analytical Manual, 8th Edition, Revision A, 1998).Before use, Dap-4C medium was added 3.5 ml sterile 50% (NH₄)₂HPO₄ and 5ml sterile 20% Lactic Acid per 150 ml medium.

KU6 trace metals solution was composed of 0.13 g NiCl₂, 2.5 gCuSO₄.5H₂O, 13.9 g FeSO₄.7H₂O, 8.45 g MnSO₄.H₂O, 6.8 g ZnCl₂, 3 g CitricAcid, and deionized water to 1 liter.

TABLE 1 Composition of Model Detergent A Detergent ingredients Wt %Linear alkylbenzenesulfonic acid (LAS) (Marlon AS3) 13 Sodiumalkyl(C12)ether sulfate (AEOS) (STEOL CS-370 E) 10 Coco soap (Radiacid631) 2.75 Soy soap (Edenor SJ) 2.75 Alcohol ethoxylate (AEO) (Bio-SoftN25-7) 11 Sodium hydroxide 2 Ethanol 3 Propane-1,2-diol (MPG) 6 Glycerol2 Triethanolamine (TEA) 3 Sodium formate 1 Sodium citrate 2Diethylenetriaminepentakis(methylenephosphonic acid) 0.2 (DTMPA)Polycarboxylate polymer (PCA) (Sokalan CP-5) 0.2 Water Up to 100 Finaladjustment of pH to pH 8 with NaOH or citric acid

TABLE 2 Composition of Model Liquid Detergent B Detergent ingredients Wt% Linear alkylbenzenesulfonic acid (LAS) 7.2 Sodium alkyl(C12)ethersulfate (AEOS) (SLES) 4.2 Coco soap (Radiacid 631) 2.75 Soy soap (EdenorSJ) 2.75 Alcohol ethoxylate (AEO) (Bio-Soft N25-7) 6.6 Sodium hydroxide1.2 Ethanol 3 Propane-1,2-diol (MPG) 6 Glycerol 2 Triethanolamine (TEA)3 Sodium formate 1 Sodium citrate 2Diethylenetriaminepentakis(methylenephosphonic acid) 0.2 (DTMPA)Polycarboxylate polymer (PCA) (Sokalan CP-5) 0.2 Water Up to 100Wash AssaysAutomatic Mechanical Stress Assay (AMSA) for Laundry

In order to assess the wash performance in laundry washing experimentsare performed, using the Automatic Mechanical Stress Assay (AMSA). Withthe AMSA, the wash performance of a large quantity of small volumeenzyme-detergent solutions can be examined. The AMSA plate has a numberof wells for test solutions and a lid firmly squeezing the laundrysample, the textile to be washed against all the slot openings. Duringthe washing time, the plate, test solutions, textile and lid arevigorously shaken at the controlled temperature to bring the testsolution in contact with the textile and apply mechanical stress in aregular, periodic oscillating manner. For further description seeWO02/42740 especially the paragraph “Special method embodiments” at page23-24.

The wash performance is measured as the brightness of the colour of thetextile washed. Brightness can also be expressed as the intensity of thelight reflected from the sample when illuminated with white light. Whenthe sample is stained the intensity of the reflected light is lower,than that of a clean sample. Therefore the intensity of the reflectedlight can be used to measure wash performance.

Colour measurements are made with a professional flatbed scanner (KodakiQsmart, Kodak, Midtager 29, DK-2605 Brøndby, Denmark, or EpsonExpression 10000XL, Epson Danmark, Transformervej 6, 2730 Herlev,Denmark), which is used to capture an image of the washed textile.

To extract a value for the light intensity from the scanned images,24-bit pixel values from the image are converted into values for red,green and blue (RGB). The intensity value (Int) is calculated by addingthe RGB values together as vectors and then taking the length of theresulting vector:Int=√{square root over (r ² +g ² +b ²)}Mini Launder-O-Meter (MiniLOM) Assay

The miniLOM assay is a small scale version of the Launder-O-Meter (LOM).It can be used to determine the “enzyme detergency benefit”. A miniLOMbasically consists of closed test tubes being rotated in a heatingcabinet at a given time and temperature. Each test tube constitutes onesmall washing machine and during an experiment, each will contain asolution of a specific detergent/enzyme system to be tested along withthe soiled and unsoiled fabrics it is tested on. Mechanical stress isachieved by the tubes being rotated and by including metal balls in thetube.

The small scale model wash system is mainly used in testing ofdetergents and enzymes at European wash conditions.

Evaluation of Stains from Mini-LOM

Wash performance is expressed as a remission value (Rem). After washingand rinsing the swatches were spread out flat and allowed to air dry atroom temperature over night. All washes are evaluated shall be evaluatedday 2 after wash. Light reflectance evaluations of the swatches weredone using a Macbeth Color Eye 7000 reflectance spectrophotometer withvery small aperture. The measurements were made without UV in theincident light and remission at 460 nm was extracted. Measurements weremade on washed swatches. The test swatch to be measured was placed ontop of another swatch of same type and colour (twin swatch). With onlyone swatch of each kind per beaker, a swatch from a replicate wash wasused in this way. The enzyme performance can be seen by comparing theremission value of using no enzyme to the remission value using one ormore enzymes. The higher the remission vale, the better the cleaningeffect.

Activity Assays

Xanthan Lyase Activity Assay (Xanthan Lyase Specific Assay)

0.8 mL 100 mM HEPES buffer, pH 6.0 was mixed with 0.2 mL Xanthan gum (5mg/mL) dissolved in water in a 1 mL 1 cm cuvette. The cuvette wasinserted into a spectrophotometer (Agilent G1103A 8453A, CA, USA) withtemperature control set at 40° C. The solution was pre-incubated for 10min and 0.1 mL sample was added and the solution was mixed by aspiringand dispensing the solution for at least 5 times using a pipette. Totalreaction volume was 1.1 mL. Absorbance at 235 nm was collected for 10min using a 30 sec measuring interval. Initial activity was calculatedby using the software (UV-Visible Chemstation Rev A.10.01 [81],Agilent).

Example 1 Identification of the GH9 Xanthanase Gene

Four bacterial strains were isolated from soil samples obtained fromdiverse places (see table 3 below) by using xanthan gum as sole carbonsource.

TABLE 3 Isolation of bacterial strains Strain Identification numberSource Country Paenibacillus sp NN062047 forest soil ChinaMicrobacterium sp NN062149 field soil Spain Microbacterium sp NN062148sand beach Denmark Microbacterium sp NN062045 garden soil Denmark

Chromosomal DNA of four bacterial strains was isolated by QIAamp DNABlood Mini Kit (Qiagen, Hilden, Germany). 2 ug of chromosomal DNA wassubjected to partial shotgun genome sequencing, a service that iscommercially available at FASTERIS SA, Switzerland. The genome sequencewas analyzed for protein sequences that have glycosyl hydrolase domains(according to the CAZY definition above). One gene and correspondingprotein sequence was identified from each bacterial strain (SEQ ID NO:1, 9, 11, and 13) and proven here to in fact have the desired activityon xanthan gum.

Example 2 Cloning and Expression of GH9 in Bacillus subtilis withN-Terminal His Tag

The gene fragments of the GH9 gene were amplified from chromosomal DNAof the four bacterial strains with specific primers D88F-forward andD89R-reverse for Paenibacillus sp NN062047; D124F-forward andD125R-reverse for Microbacterium sp NN062149; D126F-forward andD127R-reverse for Microbacterium sp NN062148; D128F-forward andD129R-reverse for Microbacterium sp NN062045 (see table 4 for sequencedetails). The primers contain overhang to cloning vector, which is aderivative of the plasmid C6221 (described in WO2012/025577), modifiedby introducing a poly histidine tag (HHHHHHPR) after the secretionsignal.

TABLE 4 Primers used for PCR amplification Amplification of GH9 gene ofSpecific primer forward Specific primer reverse Paenibacillus sp D88F:D89R: NN062047 5′TCACCATCATCCTAGGATCGCAGG 5′TTATTGATTAACGCGTTTACGGAACGTGGTTCAAAGCGTGAATGTC 3′ CTGGAACAAGCTGAATGAAATC 3′ (SEQ ID NO: 21) (SEQID NO: 22) Microbacterium D124F: D125R: sp NN0621495′TCACCATCATCCTAGGGCGACGAT 5′TTATTGATTAACGCGTTCATCCGA CGAACGCGTCGCCGTCA3′ CGACCACTCCGGTCACG 3′ (SEQ ID NO: 23) (SEQ ID NO: 24) MicrobacteriumD126F: D127R: sp NN062148 5′TCACCATCATCCTAGGGCGACGAT5′TTATTGATTAACGCGTCTACTGAA CACACAGGTCGCGGTGA 3′ CGACCACCCCCGTCGTG 3′(SEQ ID NO: 25) (SEQ ID NO: 26) Microbacterium D128F: D129R: sp NN0620455′TCACCATCATCCTAGGGCCACCAT 5′TTATTGATTAACGCGTTCAGCCGA CGAGGAAGTCACGGTGA3′ CGGCGACGCCGGACACC 3′ (SEQ ID NO: 27) (SEQ ID NO: 28)

The PCR fragments were cloned in the plasmid digested with AvrII andMluI enzymes using the In-Fusion HD cloning kit (Clontech product number639648) following the instructions from the manufacturer (PT5162-1).

The GH9 polypeptide were expressed with the secretion signal with thefollowing amino acid sequence (MKKPLGKIVASTALLISVAFSSSIASA, (SEQ ID NO:29)) replacing the native secretion signal resulting in the recombinantgene and protein sequence. (By doing so, the mature polypeptides wereexpressed with a poly histidine-tag (HHHHHHPR (SEQ ID NO: 30)) operablylinked to the mature GH9 Xanthanase.

The In-Fusion reactions were transformed in E. coli and ampicillinresistant transformants were selected and cultivated for subsequentlyDNA plasmid preparation. 7 clones of each construct were analyzed by DNAsequencing to verify the correct DNA sequence of the constructs. Thenucleotide sequence of the fusion products corresponds to SEQ ID NO: 5,SEQ ID NO: 15, SEQ ID NO: 17 and SEQ ID NO: 19. The translated proteinsequence corresponds to SEQ ID NO: 6, SEQ ID NO: 16, SEQ ID NO: 18 andSEQ ID NO: 20.

One clone with the correct recombinant gene sequence was selected andthe corresponding plasmid was integrated by homologous recombinationinto the Bacillus subtilis host cell genome and the gene construct wasexpressed under the control of a triple promoter system as described inWO99/43835. The gene coding for chloramphenicol acetyltransferase wasused as a marker (as described in Diderichsen et al., 1993, Plasmid30:312-315).

Chloramphenicol resistant transformants were analyzed by PCR to verifythe correct size of the amplified fragment. A recombinant B. subtilisclone containing the integrated expression construct was selected andgrown in liquid culture. The enzyme containing supernatant was harvestedand the enzyme was purified as described in Example 5.

Example 3 Identification, Genome Sequencing and Identification of theXanthan Lyase Gene

The Paenibacillus strain NN018054 was isolated from a soil sample fromNew Zealand by using xanthan gum as sole carbon source. Chromosomal DNAof the bacterial strain Paenibacillus NN018054 was isolated by QIAampDNA Blood Mini Kit” (Qiagen, Hilden, Germany). 2 ug of chromosomal DNAwas sent for genome sequencing at FASTERIS SA, Switzerland. The genomewas sequenced by Illumina Sequencing. The genome sequence was analyzedand the XL protein was identified (SEQ ID NO: 3) by BLASTP searches.

Example 4 Cloning and Expression of Xanthan Lyase in Bacillus subtiliswith N-Terminal His Tag

The truncated xanthan lyase gene was amplified from chromosomal DNA ofthe Paenibacillus strain NN018054 with gene specific primers (D117F: 5′TCACCATCATCCTAGGGCGGAGGCGTCCGACATGTTCGACG 3′ (SEQ ID NO: 31) (and D118R:5′ TTATTGATTAACGCGTTTACGGCTGCTGCGCGCCGGTCAGG 3′ (SEQ ID NO: 32)). Theprimers contain overhang to cloning vector, which is a derivative of theplasmid C6221 (described in WO2012/025577), modified by introducing apoly histidine tag (HHHHHHPR (SEQ ID NO: 30)) after the secretionsignal.

The PCR fragment was cloned in the plasmid digested with AvrII and MluIenzymes using the In-Fusion HD cloning kit (Clontech 639648) followingthe instructions from the manufacturer (PT5162-1).

The truncated xanthan lyase protein was expressed with the secretionsignal with the following amino acid sequence(MKKPLGKIVASTALLISVAFSSSIASA, (SEQ ID NO: 29)) replacing the nativesecretion signal resulting in the recombinant gene and protein sequenceSEQ ID NO: 7 and SEQ ID NO: 8. By doing so, the mature polypeptide wasexpressed with a poly histidine-tag (HHHHHHPR (SEQ ID NO: 30)) operablylinked to the mature xanthan lyase.

The In-Fusion reaction was transformed in E. coli and the ampicillinresistant transformants were selected and cultivated for subsequentlyDNA plasmid preparation. 7 clones were analyzed by DNA sequencing toverify the correct DNA sequence of the construct. The nucleotidesequence of the fusion product corresponds to SEQ ID NO: 7. Thetranslated protein sequence corresponds to SEQ ID NO: 8

One clone with the correct recombinant gene sequence was selected andthe corresponding plasmid was integrated by homologous recombinationinto the Bacillus subtilis host cell genome. The gene construct wasexpressed under the control of a triple promoter system (as described inWO99/43835). The gene coding for chloramphenicol acetyltransferase wasused as a marker (as described in Diderichsen et al., 1993, Plasmid30:312-315)

Chloramphenicol resistant transformants were analyzed by PCR to verifythe correct size of the amplified fragment. A recombinant B. subtilisclone containing the integrated expression construct was selected andgrown in liquid culture. The enzyme containing supernatant was harvestedand the enzyme was purified as described in Example 5.

Example 5 Purification of the GH9 and Xanthan Lyase Protein

A Bacillus subtilis strain was constructed as described in examples 2and 4 to express the protein to the culture medium. The culture brothwas centrifuged (17.696×g, 30 min) and the supernatant was carefullydecanted from the precipitate. The supernatant was filtered through aNalgene 0.2 μm filtration unit in order to remove the rest of theBacillus host cells.

The volume was reduced using a Filtron system with 10K cut off filter.The volume was reduced to approx 80 mL, followed by addition of BufferA: 50 mM TRIS+10 mM Imidazole pH 8.0 to the sample. The pH on the samplewas adjusted to 8 and applied to a Ni-NTA Superflow column (QIAGEN)equilibrated in: Buffer A. After loading, the column is washed withBuffer A for 3 column volumes (CV). Then a step gradient to 100% BufferB: Buffer B: 50 mM MES+10 mM Imidazole pH 7.0 was applied andconsecutively a second gradient is applied up to 100% Buffer C: 50 mMMES+1 M Imidazole pH 7.0 in 4 CV. All the positive fractions are run onSDS-PAGE and the respective proteins are identified by the bands. Thefractions containing XL or GH9 respectively were pooled and desaltedinto Buffer Tris 20 mM pH 7.0.

For further purification the respective pool was loaded into aQ-Sepharose Ion Exchange column (GE Healthcare) equilibrated in 20 mMTris pH 7.0. After loading, the protein was eluted using 0-100% 20 mMTris+1M NaCl, pH 7.0. The positive fractions were run on a SDS-PAGE Geland desalted into 20 mM Tris pH 7.0.

The concentration of the purified proteins was determined by Absorbanceat 280 using the respective extinction coefficients calculated from thededuced amino acids sequences of the mature proteins.

Example 6 Activity Screening of Xanthan Lyase and GH9 on Xanthan Gum

Xanthan Lyase Activity

Xanthan lyase activity was determined as described above on the purifiedxanthan lyase protein. The data is presented in the table 5 below.

TABLE 5 Specific Activity of Xanthan Lyase of SEQ ID NO: 8 Conc xanthanlyase Initial activity Specific activity in cuvette (μg/mL) (mAU/min)(mAU/min/mg enzyme) 0.291 17.274 4907 0.582 34.98 4969 1.455 94.32 5359

The data shows that the xanthan lyase had activity on xanthan gum.

Reducing Ends

The method used to determine the amount of reducing ends produced wasthe 2,2′ bicinchoninic acid assay (BCA) as described in Murphy et al.,2012, J. Biol. Chem. 287: 1252-1260 and adapted from Zhang et al, 2005,Biomacromolecules 6: 1510-1515 and Dubois et al, 1956, Anal. Chem. 28:350-356. Quantification of reducing ends was based on a glucose standardcurve. Appropriate substrate and enzyme controls were included andcorrected for in each analysis. Appropriate dilutions were used toensure samples were within the glucose calibration curve range. Theresults are shown in table 7 below.

Viscosity Reduction

The viscosity measurements were performed using the Novozymes-developedviscosity pressure assay described in WO2011/107472. 100 μL of each 1 mLhydrolysis or control was the sample size. Results presented are theaverage of three measurements and are shown in table 6 below.

Hydrolysis

The hydrolysis conditions were as follows: 40° C., 0.25% xanthan gum(XG) in 50 mM MES buffer+0.01% triton x-100 pH 7.0. Enzyme was addedupon thermal equilibration. Prior to use all enzymes were buffer changedto the MES buffer using NAP 5 columns (GE Healthcare).

Enzyme Doses

The purified enzyme preparations of example 5 were used for the analysisin following concentrations:

GH9 (SEQ ID NO: 6): 7.25 mg/L

Xanthan lyase (SEQ ID NO: 8): 40 μg/L

TABLE 6 Viscosity measurements of the GH9 (SEQ ID NO: 6) and/or XanthanLyase (SEQ ID NO: 8) on xantham gum Incubation Time 5 min 30 min 3 hoursAverage Average Average (Pa) S.D. (Pa) S.D. (Pa) S.D. Buffer (control)586 49 508 15 541 17 Xanthan gum (control) 1039 15 1012 38 971 26Xanthan gum + GH 9 946 12 995 106 911 20 Xanthan gum + xanthan lyase1023 20 1048 110 884 25 Xanthan gum + xanthan lyase + 940 30 795 20 57784 GH 9

TABLE 7 Reducing Ends Results using GH9 (SEQ ID NO: 6) and/or XanthanLyase (SEQ ID NO: 8) Incubation Time 3 hours Conditions μM glucoseequivalents Xanthan gum + GH 9 20 Xanthan gum + xanthan lyase 1312Xanthan gum + xanthan lyase + GH 9 2313

The above results from table 5 show that combination of xanthan lyaseand GH9 can degrade xanthan gum by reducing the viscosity of the media.These results are in accordance with the results obtained from thereducing ends assay, shown in table 6, which shows that the number ofreducing ends increases by the addition of xanthan lyase or xanthanlyase+GH 9, since the xanthan gum is degraded by the enzymes.

Example 7 Demonstration of Synergy Between GH9 Endoglucanase and XanthanLyase

A method using liquid chromatography was used to demonstrate thede-polymerizing effect of GH9 endoglucanase and xanthan lyase, having onxanthan gum. For this example the His-tagged xanthan lyase having SEQ IDNO: 8 and the His-tagged GH9 endoglucanase having SEQ ID NO: 6 wereused. The enzymes were purified as described in example 5.

Substrate mixture consisting of 0.25% (w/v) xanthan gum (Keltron) in thereaction buffer 100 mM HEPES buffer, pH 6.0 supplemented with 0.01%(w/v) Triton-X was mixed with 0.02 mg/mL xanthan lyase and 0.02 mg/mLGH9. 50 μL samples were withdrawn at fixed time point and the sampleswere diluted with 150 μL HEPES buffer, pH 6.0. The sample wasimmediately injected using a 100 μL sample loop and separated on a 26 mLSuperdex S200 column (GE Healthcare, Uppsala, Sweden). The system usedin this experiment was an ÄKTA Explorer (GE healthcare) placed in a coldroom (+4° C.). Separation of polysaccharides was conducted at a flowrate of 0.7 mL/min and using 0.1 M HEPES, pH 7.0 buffer. Absorbance at235 nm was monitored to detect the double bond of the xanthan lyasereaction product. Two peaks could be observed in the chromatogramseluting at retention volumes 9 and 19 mL. A control sample consisting of0.02 mg/mL xanthan lyase and 0.25% (w/v) xanthan gum incubated for 3 hin the reaction buffer only gave rise to a peak with retention volume of9 mL. Thus, the peak appearing at 9 mL corresponded to xanthan lyasetreated xanthan gum. Over time the 9 mL peak decreased while the peakeluting at 19 mL increased in size. The results are presented in table 8below.

TABLE 8 Chromatographic results of GH9 (SEQ ID NO: 6) and Xanthan Lyase(SEQ ID NO: 8) on xanthan gum Peak height 9 mL Peak height 19 mL Time(min) (mAU) (mAU) 3 36 5 40 20 15 85 11 20

The data indicated that the combination of xanthan lyase and the GH9endoglucanase can degrade xanthan gum to smaller xanthan gum derivedoligosaccharides.

Example 8 Specific Activity of Xanthan Lyase Treated Xanthan Gum Vs CMC

The method used to determine the specific activity for a GH9endoglucanase was the p-hydroxybenzoic acid method (PHBAH). For thisexample the His-tagged GH9 endoglucanase derived from Paenibacillus sp.and having the sequence of SEQ ID NO: 6 was used.

Quantification of reducing ends was based on a glucose standard curve.The specific activity on carboxymethyl-cellulose 7LF (Hercules) wasdetermined by using a substrate concentration of 1% w/v. The specificactivity on xanthan lyase treated xanthan gum (prepared according toNankai et al. (1999) from the source Keltran) was determined using a0.25% w/v solution. Assay buffer was 0.1 M HEPES, pH 7.0. 1.5 mLsubstrate dissolved in the assay buffer was pre-heated in glass tubesfor 5 min. 0.5 mL appropriate enzyme dilution was added and the samplewas mixed by a vortex for 10 sec. The samples were incubated for 20 minat 40° C. The enzymatic reaction was terminated by adding 1.0 mL stopreagent consisting of 1.5 g PHBAH, 5 g K/Na tartrate dissolved in 100 mL2% w/v NaOH. The samples were boiled for 10 min and 200 μL weretransferred from each tube to a 96-hole microtiter plate. Absorbance at410 nm was collected. Absorbance values were converted to IU by usingthe glucose standard curve. One IU is defined as the release of 1 μmolglucose equivalent formed per min at 40° C. and pH 7.0. The results areshown in table 9 below.

TABLE 9 Specific activity of the GH9 (SEQ ID NO: 6) on CMC compared toxanthan lyase treated xanthan gum Substrate Specific activity (IU/mg)CMC 2.1 Xanthan lyase treated xanthan gum 41.5

The results show that the GH9 endoglucanase is more active on xanthanlyase treated xanthan gum compared to CMC.

Reference

Nankai, H., Hashimoto, W., Miki, H., Kawai, S., Murata, K. (1999)“Microbial system for polysaccharide depolymerization: enzymatic routefor xanthan depolymerization by Bacillus sp. Strain GL1”, Applied andEnvironmental Microbiology, Vol 65(6), p. 2520-2526.

Example 9 AMSA Wash Performance of Xanthan Lyase (SEQ ID NO: 8) and/orGH9 (SEQ ID NO: 6)

The experiments were conducted as described in the Automatic MechanicalStress Assay (AMSA) for laundry method using a 2 cycle wash procedureand the experimental conditions specified in tables 10 and 11 below: Theenzyme(s) as stated in tables 12 and 13 below were added in cycle 1.

TABLE 10 Conditions for Cycle 1 Test solution Buffer (50 mM MES) Testsolution volume 160 micro L pH Adjusted to pH 7 Wash time 30 minutesTemperature 20° C. or 40° C. Water hardness 15° dH Ca²⁺:Mg²⁺:CO₃ ²⁻ratio 4:1:7.5 Swatch DN31: Xanthan gum with carbon black

TABLE 11 Conditions for Cycle 2 Test solution 3.33 g/L model detergent ATest solution volume 160 micro L pH Unadjusted Wash time 30 minutesTemperature 20° C. or 40° C. Water hardness 15° dH Ca²⁺:Mg²⁺:CO₃ ²⁻ratio 4:1:7.5

Water hardness was adjusted by addition of CaCl₂, MgCl₂, and NaHCO₃ tothe test system. After washing the textiles were flushed in tap waterand air-dried. The swatches were prepared by adding xanthan gum fromXanthomonas campestris (Sigma cat #C1253) mixed with carbon black to acotton fabric.

TABLE 12 Results of Xanthan Lyase (SEQ ID NO: 8) and/or GH9 (SEQ ID NO:6) at 20° C. in AMSA assay. Enzyme(s) added (mg enzyme protein/ L washsolution) Intensity (Avg) Std dev No enzyme added 392.38 1.80 XanthanLyase (1.0 mg EP/L) 396.72 1.99 GH9 (0.25 mg EP/L) 398.46 1.51 XanthanLyase (1.0 mg EP/L) & 407.11 1.57 GH9 (0.25 mg EP/L)

TABLE 13 Results of Xanthan Lyase (SEQ ID NO: 8) and/or GH9 (SEQ ID NO:6) at 40° C. in AMSA assay Enzyme(s) added Intensity (Avg) Std dev Noenzyme added 393.41 1.41 Xanthan Lyase (1.0 mg EP/L) 402.13 2.41 GH9(0.25 mg EP/L) 401.56 1.24 Xanthan Lyase (1.0 mg EP/L) & 411.91 0.99 GH9(0.25 mg EP/L)

These results show that combination of xanthan lyase and GH9 has awashing effect under the conditions tested. Also GH9 alone performswell, whereas xanthan lyase alone only has minor effect in this assay.

Example 10 Xanthan Degrading Activity of GH9 Enzymes and Xanthan Lyaseby Measurement of Viscosity Reduction

Viscosity Reduction

The viscosity measurements were performed using the Novozymes-developedviscosity pressure assay described in WO2011/107472. 400 μL was thesample size. Results presented are the average of three measurements andare shown in table 14 below.

Hydrolysis

The hydrolysis conditions were as follows: 30° C., 0.25% xanthan gum(XG) in 50 mM MES buffer+0.01% triton x-100 pH 7.0. Enzyme was addedupon thermal equilibration. Prior to use all enzymes were buffer changedto the MES buffer using NAP 5 columns (GE Healthcare).

Enzyme Doses

The purified enzyme preparations of example 5 were used for the analysisat 31.25 mg/L. The enzyme mixtures of xanthan lyase (SEQ ID NO: 8) andGH9 endoglucanases were tested in duplicates.

TABLE 14 Viscosity measurements of different GH9's (SEQ ID NOs: 6, 16,18 or 20) and/or Xanthan Lyase (XL, SEQ ID NO: 8) on xantham gum T = 30T = 0 minutes minutes T = 1 hour T = 2 hours T = 3 hours T = 4 hoursAverage Average Average Average Average Average Sample (Pa) S.D (Pa) S.D(Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D Xanthan Gum 935 40 905 29 1065 206845 35 765 6 755 32 (control) Buffer control 542 26 572 110 555 15 49857 482 104 435 71 Xanthan gum + 962 40 898 21 952 114 832 17 862 106 81551 xanthan lyase (XL) Xanthan gum + GH9 992 10 945 6 925 6 882 10 915 78902 104 (SEQ ID NO: 6) Xanthan gum + GH9 1042 10 985 15 1025 93 935 6938 86 895 12 (SEQ ID NO: 16) Xanthan gum + GH9 1048 25 1062 130 985 21955 21 932 53 908 38 (SEQ ID NO: 18) Xanthan gum + GH9 1042 20 1028 311038 98 942 20 912 20 855 47 (SEQ ID NO: 20) Xanthan gum + 925 45 578 42572 62 515 21 482 44 412 70 XL + GH9 (SEQ ID NO: 6) Xanthan gum + 975 97628 12 625 75 502 30 418 21 408 71 XL + GH9 (SEQ ID NO: 16) Xanthangum + 948 21 808 6 782 10 708 32 632 17 645 21 XL + GH9 (SEQ ID NO: 18)Xanthan gum + 908 15 712 17 668 31 592 20 592 70 472 0 XL + GH9 (SEQ IDNO: 20)

The results presented above show that the combination of the differentGH9 with xanthan lyase can degrade the xanthan present in the media,thus leading to viscosity reduction.

Example 11 Cloning and Expression of GH9 in Bacillus subtilis withoutN-Terminal His Tag

The gene fragments of the GH9 gene were amplified from chromosomal DNAof the four bacterial strains with specific primers D158F-forward andD159R-reverse for Paenibacillus sp NN062047; D168F-forward andD169R-reverse for Microbacterium sp NN062149; D170F-forward andD170R-reverse for Microbacterium sp NN062148; D171F-forward andD172R-reverse for Microbacterium sp NN062045 (see table 15 for sequencedetails). The primers contain overhang to cloning vector, C6221(described in WO2012/025577), after the secretion signal.

TABLE 15 Primers used for PCR amplification Amplification of GH9 gene ofSpecific primer forward Specific primer reverse Paenibacillus D158F: 5′D159R: 5′ sp NN062047 GCTTTTAGTTCATCGATCGCATCGGC TTATTGATTAACGCGTTTACGGATATCGCAGGCGTGGTTCAAAGCGTG ACTGGAACAAGCTGAATGAAA 3′ A 3′ (SEQ ID NO: 34)(SEQ ID NO: 33) Microbacterium D168F: 5′GCTTTTAGTTCATCGATCGC D169R: 5′sp NN062149 ATCGGCTGCGACGATCGAACGCGTC TTATTGATTAACGCGTTCATCCG GCCGTCA 3′ACGACCACTCCGGTCACG 3′ (SEQ ID NO: 35) (SEQ ID NO: 36) MicrobacteriumD170F: 5′ D170R: 5′ sp NN062148 GCTTTTAGTTCATCGATCGCATCGGCTTATTGATTAACGCGTCTACTGA TGCGACGATCACACAGGTCGCGGTG ACGACCACCCCCGTCGTG 3′A 3′ (SEQ ID NO: 38) (SEQ ID NO: 37) Microbacterium D171F: 5′ D172R: 5′spNN062045 GCTTTTAGTTCATCGATCGCATCGGC TTATTGATTAACGCGTTCAGCCGTGCCACCATCGAGGAAGTCACGGTG ACGGCGACGCCGGACACC 3′ A 3′ (SEQ ID NO: 40)(SEQ ID NO: 39)

The PCR fragment was cloned in the plasmid digested with ClaI and MluIenzymes using the In-Fusion HD cloning kit (Clontech product number639648) following the instructions from the manufacturer (PT5162-1).

The GH9 protein was expressed with the secretion signal with thefollowing amino acid sequence (MKKPLGKIVASTALLISVAFSSSIASA (SEQ ID NO:29)) replacing the native secretion signal resulting in the recombinantgene and protein sequence.

The In-Fusion reaction was transformed in E. coli and ampicillinresistant transformants were selected and cultivated for subsequentlyDNA plasmid preparation. 7 clones were analyzed by DNA sequencing toverify the correct DNA sequence of the construct.

One clone with the correct recombinant gene sequence was selected andthe corresponding plasmid was integrated by homologous recombinationinto the Bacillus subtilis host cell genome and the gene construct wasexpressed under the control of a triple promoter system as described inWO99/43835. The gene coding for chloramphenicol acetyltransferase wasused as a marker (as described in Diderichsen et al., 1993, Plasmid30:312-315).

Chloramphenicol resistant transformants were analyzed by PCR to verifythe correct size of the amplified fragment.

Example 12 Cloning and Expression of Xanthan Lyase in Bacillus subtiliswithout N-Terminal His Tag

The truncated xanthan lyase gene was amplified from chromosomal DNA ofthe Paenibacillus strain NN018054 with gene specific primers (D160F: 5′GCTTTTAGTTCATCGATCGCATCGGCTGCGGAGGCGTCCGACATGTTCGACG 3′ (SEQ ID NO: 41))and D161R: 5′ TTATTGATTAACGCGTTTACGGCTGCTGCGCGCCGGTCAGG 3′ (SEQ ID NO:42)). The primers contain overhang to cloning vector, C6221 (describedin WO2012/025577), after the secretion signal.

The PCR fragment was cloned in the plasmid digested with ClaI and MluIenzymes using the In-Fusion HD cloning kit (Clontech 639648) followingthe instructions from the manufacturer (PT5162-1).

The xanthan lyase protein was expressed with the secretion signal withthe following amino acid sequence (MKKPLGKIVASTALLISVAFSSSIASA, (SEQ IDNO. 29)) replacing the native secretion signal resulting in therecombinant gene and protein sequence.

The In-Fusion reaction was transformed in E. coli and ampicillinresistant transformants were selected and cultivated for subsequentlyDNA plasmid preparation. 7 clones were analyzed by DNA sequencing toverify the correct DNA sequence of the construct.

One clone with the correct recombinant gene sequence was selected andthe corresponding plasmid was integrated by homologous recombinationinto the Bacillus subtilis host cell genome and the gene construct wasexpressed under the control of a triple promoter system as described inWO99/43835. The gene coding for chloramphenicol acetyltransferase wasused as a marker (as described in Diderichsen et al., 1993, Plasmid30:312-315).

Chloramphenicol resistant transformants were analyzed by PCR to verifythe correct size of the amplified fragment.

Example 13 Construction of an Aspergillus oryzae Expression VectorContaining the Sequence Encoding a C-Terminal Truncated Xanthan LyasePolypeptide Having Xanthanase Activity

Two synthetic oligonucleotide primers shown below were designed to PCRamplify the xanthan lyase gene, having SEQ ID NO: 4, from the genomicDNA prepared from Paenibacillus sp. NN018054. An IN-FUSION™ Cloning Kit(BD Biosciences, Palo Alto, Calif., USA) was used to clone the fragmentdirectly into the expression vector pDau109 (WO 2005/042735).

F-C3AQX (SEQ ID NO: 43) 5′-GGTGAAGCGTACGCGT GCGGAGGCGTCCGACATGTT-3′R-C3AQX (SEQ ID NO: 44) 5′-AGATCTCGAGAAGCTT TTACGGCTGCTGCGCGCCGG-3′

Bold letters represent gene sequence. The underlined sequence ishomologous to the insertion sites of pDau109.

An MJ Research PTC-200 DNA engine was used to perform the PCR reaction.A Phusion® High-Fidelity PCR Kit (Finnzymes Oy, Espoo, Finland) was usedfor the PCR amplification. The PCR reaction was composed of 4 μl of 5×GCbuffer (Finnzymes Oy, Espoo, Finland), 0.4 μl of dNTPs (10 mM), 0.2 μlof Phusion® DNA polymerase (0.2 units/μl) (Finnzymes Oy, Espoo,Finland), 1 μl of primer F-C3AQX (10 μM), 1 μl of primer R-C3AQX (10μM), 0.5 μl of genomic DNA (100 ng/μl), and 12.9 μl of deionized waterin a total volume of 20 μl. The PCR conditions were 1 cycle at 98° C.for 1 minute. 30 cycles each at 98° C. for 10 seconds and 72° C. for 1.5minutes; and 1 cycle at 72° C. for 5 minutes. The sample was then heldat 10° C. until removed from the PCR machine.

The reaction products were isolated by 1.0% agarose gel electrophoresisusing 40 mM Tris base, 20 mM sodium acetate, 1 mM disodium EDTA (TAE)buffer where a 2283 bp product band was excised from the gel andpurified using an illustra GFX® PCR DNA and Gel Band Purification Kit(GE Healthcare Life Sciences, Brondby, Denmark) according to themanufacturer's instructions. The fragment was then cloned into Mlu I andHind III digested pDau109 (WO 2005/042735) using an IN-FUSION™ CloningKit resulting in plasmid pC3AQX. Cloning of the C3AQX gene into MluI-Hind III digested pDau109 resulted in the transcription of thePaenibacillus sp-18054 C3AQX gene under the control of a NA2-tpi doublepromoter. The nucleotide sequence and deduced amino acid sequence of thePaenibacillus sp-18054 xanthan lyase C3AQX gene is shown in SEQ ID NO:45 and SEQ ID NO: 46, respectively.

The cloning protocol was performed according to the IN-FUSION™ CloningKit instructions generating a C3AQX xanthan lyase construct. The treatedplasmid and insert were transformed into One Shot® TOP10F′ ChemicallyCompetent E. coli cells (Invitrogen, Carlsbad, Calif., USA) according tothe manufacturer's protocol and plated onto LB plates supplemented with0.1 mg of ampicillin per ml. After incubating at 37° C. overnight,colonies were seen growing under selection on the LB ampicillin plates.Two colonies transformed with the C3AQX xanthan lyase construct werecultivated in LB medium supplemented with 0.1 mg of ampicillin per mland plasmid was isolated with a QIAprep Spin Miniprep Kit (QIAGEN Inc.,Valencia, Calif., USA) according to the manufacturer's protocol.

Isolated plasmids were sequenced with vector primers and C3AQX genespecific primers in order to determine a representative plasmidexpression clone that was free of PCR errors.

Example 14 Expression of the Paenibacillus sp-18054 Xanthan Lyase inAspergillus

The expression plasmid pC3AQX was transformed into Aspergillus oryzaeMT3568. Aspergillus oryzae MT3568 is an AMDS (acetamidase) disruptedderivative of JaL355 (WO 2002/40694) in which pyrG auxotrophy wasrestored in the process of knocking out the A. oryzae acetamidase (AMDS)gene. MT3568 protoplasts are prepared according to the method ofEuropean Patent, EP0238023, pages 14-15, which are incorporated hereinby reference.

Transformants were purified on COVE sucrose selection plates throughsingle conidia prior to sporulating them on PDA plates. Production ofthe Paenibacillus sp-18054 xanthan lyase polypeptide by thetransformants was analyzed from culture supernatants of 0.75 ml 96 deepwell stationary cultivations at 30° C. in YP+2% glucose medium.Expression was verified on an E-Page 8% SDS-PAGE 48 well gel(Invitrogen, Carlsbad, Calif., USA) by Coomassie staining. Onetransformant was selected for further work and designated Aspergillusoryzae XL-4.

For larger scale production, Aspergillus oryzae XL-4 spores were spreadonto a PDA plate and incubated for five days at 37° C. The confluentspore plate was washed twice with 5 ml of 0.01% TWEEN® 20 to maximizethe number of spores collected. The spore suspension was then used toinoculate seven 500 ml flasks containing 100 ml of Dap-4C medium. Theculture was incubated at 30° C. with constant shaking at 100 rpm. At dayfive post-inoculation, the culture broth was collected by filtrationthrough a bottle top MF75 Supor MachV 0.2 μm PES filter (Thermo FisherScientific, Roskilde, Denmark). Fresh culture broth from thistransformant produced a band of Xanthan lyase protein of approximately90 kDa.

Strains

Aspergillus oryzae MT3568 strain was used for expression of theAcremonium alcalophilum gene encoding the polypeptide havingendoglucanase activity. A. oryzae MT3568 is an amdS (acetamidase)disrupted gene derivative of Aspergillus oryzae JaL355 (WO 2002/40694)in which pyrG auxotrophy was restored by disrupting the A. oryzaeacetamidase (amdS) gene.

Example 15 Activity Screening of Non-Tagged Xanthan Lyase (SEQ ID NO: 4)Expressed in Aspergillus oryzae

Filtered supernatant from a fermentation performed as described inexample 14 was concentrated tenfold by a Vivaspin® 20 centrifugal column(Sartorius Stedim biotech, product number VS2092). Xanthan lyaseactivity in the concentrated sample was measured by viscosity reductionand reducing ends, as described in example 6 for the purified His-taggedenzymes.

Reducing Ends

The method used to determine the amount of reducing ends produced wasthe 2,2′ bicinchoninic acid assay (BCA) as described in Murphy et al.,2012, J. Biol. Chem. 287: 1252-1260 and adapted from Zhang et al, 2005,Biomacromolecules 6: 1510-1515 and Dubois et al, 1956, Anal. Chem. 28:350-356. Quantification of reducing ends was based on a glucose standardcurve. Appropriate substrate and enzyme controls were included andcorrected for in each analysis. Appropriate dilutions were used toensure samples were within the glucose calibration curve range. Theresults are shown in table 17 below

Viscosity Reduction

The viscosity measurements were performed using the Novozymes-developedviscosity pressure assay described in WO2011/107472. 400 μL was thesample size. Results presented are the average of two measurements andare shown in table 16 below.

Hydrolysis

The hydrolysis conditions were as follows: 30° C., 0.25% xanthan gum(XG) in TY medium. Enzyme was added upon thermal equilibration.

Enzyme Doses

The purified enzyme preparations of example 5 were used for the analysisin the following final concentrations:

GH9 (SEQ ID NO: 6): 31.25 mg/L

Xanthan lyase (SEQ ID NO: 4): 31.25 mg/L

The concentration of xanthan lyase in the concentrated supernatant wasestimated to be roughly similar to the purified enzyme based on SDS-pageanalysis.

TABLE 16 Viscosity measurements T = 0 minutes T = 30 mins T = 1 hour T =2 hours Average Average Average Average Sample (Pa) S.D (Pa) S.D (Pa)S.D (Pa) S.D H₂O 436 31 486 15 436 95 434 35 Xanthan Gum (control) 129330 1261 23 1220 43 1277 23 Xanthan gum + xanthan lyase (SEQ 1131 11 82569 778 13 767 19 ID NO: 4) + GH9 (SEQ ID NO: 6) Xanthan gum + hoststrain 1200 71 1333 42 1141 68 1224 80 (concentrated supernant) Xanthangum + host strain 1125 36 1120 50 1071 53 1126 40 (concentratedsupernant) + GH9 (SEQ ID NO: 6) Xanthan gum + xanthan lyase 1225 80 100093 1040 5 1111 31 (concentrated supernatant) Xanthan gum + xanthan lyase1120 41 841 48 761 29 722 19 (concentrated supernatant) + GH9 (SEQ IDNO: 6) Xanthan gum + DAP-4C growth 1185 53 1173 94 1180 66 1169 50 media

TABLE 17 Reducing Ends Results Incubation Time 30 min Conditions μMglucose equivalents Xanthan gum + concentrated 32 supernatant from A.oryzae host strain Xanthan gum + concentrated 1451 supernatantcontaining xanthan lyase

The production of xanthan lyase in Aspergillus oryzae shows that thesecreted xanthan lyase is active on xanthan gum alone, while the stableviscosity measurements for the same system show this to be an exo-enzymeaction, having little effect on the bulk polymer backbone.

Example 16 Identification of New GH9 Xanthanases and XL Genes

Two new paenibacillus were isolated from soil samples (see table 18)following the same procedure as described in examples 1 and 3.

TABLE 18 Isolation of bacterial strains Strain Identification numbersource Country Paenibacillus sp NN062253 forest soil United StatesPaenibacillus sp NN062250 forest soil United States

Chromosomal DNA extraction and genome sequencing of the two new strainswas done as described in examples 1 and 3. The genes from the newbacterial strains as well as isolation of a new xanthan lyase and 2truncated GH9 genes from Paenibacillus NN062047 and the correspondingprotein sequences were identified and are presented in table 19.

TABLE 19 Natural genes and corresponding polypeptide ID sequencesAmplification of gene from SEQ ID NO SEQ ID NO organism of gene ofpolypeptide Paenibacillus NN062047 47 48 Paenibacillus NN062047 51 52Paenibacillus NN062253 55 56 Paenibacillus NN062250 59 60 PaenibacillusNN062047 63 64

Example 17 Cloning and Expression of GH9 and Xanthan Lyase Candidates inBacillus subtilis with N-Terminal His Tag

The gene fragments (with the corresponding translated proteins) fromexample 16 were amplified from chromosomal DNA of the bacterial strainswith specific primers (see table 20) and cloned and expressed inBacillus subtilis with N-terminal poly histidine tag (HHHHHHPR-) afterthe secretion signal as described in example 2 and 4.

TABLE 20 Primers used for PCR amplification SEQ ID NO of Amplificationpoly- of gene from: peptide Specific primer forward Specific primerreverse Paenibacillus 50 D244F D245R NN062047 TCACCATCATCCTAGGGCAGGGTTATTGATTAACGCGTTTAGG ACCGTCAGCAAAATTTCCG GTGTTGTTGCGCTAACCGGA (SEQ IDNO: 69) (SEQ ID NO: 70) Paenibacillus 54 D242F D243R NN062047TCACCATCATCCTAGGGCAGGG TTATTGATTAACGCGTTTAAG ACCGTCAGCAAAATTTCCGTCTGGTAGACCGCTGGTCCG (SEQ ID NO: 71) (SEQ ID NO: 72) Paenibacillus 58D271F D272R NN062253 TCACCATCATCCTAGGAACGCA TTATTGATTAACGCGTTTAAGAGCCTGGTTCAAAGCGTGA GGGTCACGGAAACAAGCTGA (SEQ ID NO: 73) (SEQ ID NO: 74)Paenibacillus 62 D289F D290R NN062250 TCACCATCATCCTAGGGCGGATTTATTGATTAACGCGTTTACG GAATTCGACGGGATGCGGG GATTACGTACAAATTTGACT (SEQ IDNO: 75) (SEQ ID NO: 76) Paenibacillus 66 D293F D294R NN062047TCACCATCATCCTAGGGCGGAC TTATTGATTAACGCGTTTATG GAGTTTGACACGCTAAGGGGGACCTTTACCAGCTTCACG (SEQ ID NO: 77) (SEQ ID NO: 78) Paenibacillus 68D332F D333R NN018054 TCACCATCATCCTAGGGCGGAG TTATTGATTAACGCGTTCAGTGCGTCCGACATGTTCGACG CGAGCCAGATGTAATCAAGC (SEQ ID NO: 79) (SEQ ID NO: 80)

Example 18 AMSA Wash Performance of Xanthan Lyase and GH9

The experiments were conducted as described in the Automatic MechanicalStress Assay (AMSA) for laundry method using a single cycle washprocedure and the experimental conditions specified in table 21 below.The results are given in tables 22 and 23 using 6 different GH9endoglucanases and 4 different xanthan lyases along with controls whereeither the GH9 endoglucanase and/or xanthan lyase are absent. Theresults are shown as the ΔInt enzyme value.

TABLE 21 Experimental conditions for Wash Cycle Test solution 3.33 g/LModel liquid detergent B Test solution volume 140 μL detergent per slot;20 μL enzyme per slot pH Unadjusted Wash time 20 minutes Temperature 20°C. or 40° C. Enzyme dosage Xanthan lyase: 1 mg EP/L GH9: 0.5 mg EP/LWater hardness 16° dH Ca²⁺:Mg²⁺:CO₃ ²⁻ ratio 5:1:3 Swatch DN31D. Xanthangum with carbon black

Water hardness was adjusted by addition of CaCl₂, MgCl₂, and NaHCO₃ tothe test system. After washing the textiles were flushed in tap waterand air-dried. The swatches were prepared by adding xanthan gum fromXanthomonas campestris (Food Grade Keltrol T, Kelco) mixed with carbonblack to a cotton fabric.

TABLE 22 Compiled AMSA wash data using model liquid detergent B at 40°C. Xanthan Lyase ΔInt enzyme SEQ SEQ SEQ SEQ value ID NO: ID NO: ID NO:ID NO: GH9 No XL 8 62 66 68 SEQ ID NO: 2¹ 9.6 17.8 ND² ND² ND² SEQ IDNO: 6 13.8 25.5 22.8 30.1 22.0 SEQ ID NO: 16 8.6 18.9 17.7 20.8 15.5 SEQID NO: 20 7.9 13.5 13.7 13.2 13.2 SEQ ID NO: 50 12.8 22.6 19.5 25.5 18.5SEQ ID NO: 54 4.6 14.6 12.3 18.1 13.3 SEQ ID NO: 58 10.2 14.4 13.1 15.015.8 No GH9 0 1.7 0.5 3.8 −1.4 (Control) ¹Quantification of SEQ ID NO: 2uncertain due to a second closely running band present in the SDS-gel.²Not determined

TABLE 23 Compiled AMSA wash data using model liquid detergent B at 20°C. Xanthan Lyase ΔInt enzyme SEQ SEQ SEQ SEQ value ID NO: ID NO: ID NO:ID NO: GH9 No XL 8 62 66 68 SEQ ID NO: 2¹ 4.7 7.0 ND² ND² ND² SEQ ID NO:6 10.6 16.6 19.1 22.8 15.1 SEQ ID NO: 16 5.0 14.6 14.5 15.0 9.5 SEQ IDNO: 20 3.1 10.6 9.9 9.6 6.4 SEQ ID NO: 50 8.6 16.9 15.2 17.2 11.0 SEQ IDNO: 54 3.7 13.7 13.0 14.4 9.8 SEQ ID NO: 58 8.8 14.1 13.3 12.7 10.2 NoGH9 0 5.0 3.7 3.5 1.8 (Control) ¹Quantification of SEQ ID NO: 2uncertain due to a second closely running band present in the SDS-gel.²Not determined

These results show that different combinations of GH9 endoglucanases andxanthan lyases give a synergistic wash effect on xanthan gum with carbonblack stains at both 20° C. and 40° C., thus indicating that thissynergistic effect can be extrapolated to all xanthan lyases and all GH9endoglucanases.

Example 19 MiniLOM Wash Performance of Xanthan Lyase (SEQ ID NO: 8)and/or GH9 (SEQ ID NO: 6, 16, 50, 54 or 58)

The enzymes of the present invention were tested using the miniLOM assayin order to determine the “enzyme detergency effect”. Test tubes arefilled with test solution, soiled fabrics and steel balls and rotated ina heating cabinet at a given temperature. Cleaning benefits are studiedwhen washing in either buffer or model liquid detergent A. Theexperimental conditions for the experiments are specified in Table 24.

TABLE 24 Experimental conditions for MiniLOM Test solution Model liquiddetergent A Test solution volume 40 mL pH Not adjusted Wash time 30minutes Temperature 40° C. Water hardness 16° dH Ca²⁺:Mg²⁺:CO₃ ²⁻ ratio5:1:3 Enzyme dosage Xanthan lyase: 1 mg EP/L GH9: 0.5 mg EP/L SwatchesCircular swatches 2 cm in diameter Stains 4 x Technical stains withXanthan Gum with Carbon Black (DN31D) Ballast 6 x wfk10A (100% wovencotton) 6 x wfk80A (100% knitted cotton) Total ballast weight Technicalstains: 0.43 g Ballast stains: 0.53 g pr tube Mechanics 4 stainlesssteel balls, 6 mm in diameter

Water hardness was adjusted by addition of CaCl₂, MgCl₂, and NaHCO₃ tothe test system. After washing the textiles were flushed in tap waterand air-dried. The swatches were prepared by adding xanthan gum fromXanthomonas campestris (Food Grade Keltrol T, Kelco) mixed with carbonblack to a cotton fabric.

The performance of the enzyme(s) is evaluated by measuring the remissionof the textile swatches using the ColorEye at 460 nm.

TABLE 25 Results of MimiLOM Wash using 5 different GH9s and/or XanthanLyase (SEQ ID NO: 8) SEQ ID NO of GH9 Rem₄₆₀ endoglucanase No Enzyme XLGH9 XL + GH9 SEQ ID NO: 6 40.4 ± 1.3 40.3 ± 1.3 48.1 ± 0.5 49.8 ± 0.5SEQ ID NO: 16 40.9 ± 3.2 40.2 ± 2.5 45.6 ± 0.4 47.9 ± 0.6 SEQ ID NO: 5040.6 ± 2.3 40.4 ± 1.7 45.6 ± 0.7 47.8 ± 0.7 SEQ ID NO: 54 40.1 ± 2.040.8 ± 2.7 45.4 ± 1.3 47.0 ± 0.9 SEQ ID NO: 58 41.1 ± 0.6 40.8 ± 2.247.3 ± 0.4 46.6 ± 0.3

These results show that adding the GH9 endoglucanase (all five variants)to the wash gives a significant cleaning benefit under the conditionstested. Furthermore, adding the GH9 endoglucanase (all five variants)together with XL results in an additional wash effect even though thexanthan lyase on its own has no apparent effect.

Example 20 Identification of the GH9 Xanthanase and Xanthan Lyase Genes

Six new paenibacillus sp were isolated from soil samples (see table 26)following the same procedure as described in examples 1 and 3.

TABLE 26 Identification of Bacterial Strains Strain Identificationnumber Source Country Paenibacillus sp NN062046 Forest soil ChinaPaenibacillus sp NN062408 Soil Denmark Paenibacillus sp NN062332 SoilUnited States Paenibacillus sp NN062147 Sand beach Denmark Paenibacillussp NN062193 Garden soil Denmark Microbacterium sp NN062175 Soil Denmark

Chromosomal DNA extraction and genome sequencing of the six new strainswas done as described in examples 1 and 3. The genes from the newbacterial strains as well as isolation of 6 new xanthan lyases and 8 GH9genes and the corresponding protein sequences were identified and arepresented in table 27.

TABLE 27 Natural genes and corresponding polypeptide ID sequencesAmplification of gene from SEQ ID NO of organism SEQ ID NO of genepolypeptide Paenibacillus NN062046 81 82 Paenibacillus NN018054 85 86Paenibacillus NN062408 89 90 Paenibacillus NN018054 93 94 PaenibacillusNN062332 97 98 Paenibacillus NN062147 105 106 Paenibacillus NN062193 109110 Paenibacillus NN062408 113 114 Paenibacillus NN062332 117 118Paenibacillus NN062046 121 122 Paenibacillus NN062253 125 126Microbacterium NN062175 129 130 Paenibacillus NN062193 133 134Paenibacillus NN062193 137 138

Example 21 Cloning and Expression of GH9 and Xanthan Lyase Candidates inBacillus subtilis with N-Terminal His Tag

The gene fragments (with the corresponding translated proteins) fromexample 20 were amplified from chromosomal DNA of the bacterial strainswith specific primers (see table 28) and cloned and expressed inBacillus subtilis with N-terminal poly histidine tag (HHHHHHPR-) afterthe secretion signal as described in example 2 and 4.

TABLE 28 Primers used for PCR amplification SEQ ID SEQ ID NO of NO ofAmplification recombinant poly- of gene from: gene peptide Specificprimer forward Specific primer reverse Paenibacillus 83 84 F-C597BR-C597B NN062046 TCACCATCATCCTAGGGCCG TTATTGATTAACGCGTTTA TAGCCCCGCTCCCCTGGCGTCGTTACGAGGAA (SEQ ID NO: 141) (SEQ ID NO: 142) Paenibacillus 95 96F-C5B9G R-C5B9G NN018054 TCACCATCATCCTAGGGCTC TTATTGATTAACGCGTTTACGGCTCCGCTGCCG GCCCCGCACCGTCACATC (SEQ ID NO: 143) (SEQ ID NO: 144)Paenibacillus 99 100 F-C59T2 R-C59T2 NN062332 TCACCATCATCCTAGGGCCGTTATTGATTAACGCGTCTA TGCCGCCGTTGCCG ACTTGGCGTGACGGT (SEQ ID NO: 145) (SEQID NO: 146) Paenibacillus 107 108 F-C4AM9 R-C4AM9 NN062147TCACCATCATCCTAGGGCAG TTATTGATTAACGCGTTTA ACGAATTCGATGCAATGAGGGCGGCACGAATTCAAACTTG (SEQ ID NO: 147) ACC (SEQ ID NO: 148) Paenibacillus111 112 F-C4AKF R-C4AKF NN062193 TCACCATCATCCTAGGTCAGATTATTGATTAACGCGTCTA TGAATATGATACGATGCGGG AGAGCCTGGCGCCACATA (SEQ ID NO:149) TTCA (SEQ ID NO: 150) Paenibacillus 115 116 F-C59TM R-C59TMNN062408 TCACCATCATCCTAGGTCCGA TTATTGATTAACGCGTCTA CGCGTATGATGCACTGGATCAACTCAAACTT (SEQ ID NO: 151) (SEQ ID NO: 152) Paenibacillus 119120 F-C59SY R-C59SY NN062332 TCACCATCATCCTAGGGGCG TTATTGATTAACGCGTTTAGCGAAGCGAGCGGG CGGCACATATTCAAATTTG (SEQ ID NO: 153) (SEQ ID NO: 154)Paenibacillus 123 124 F-C3AX4 R-C3AX4 NN062046 TCACCATCATCCTAGGGCGGTTATTGATTAACGCGTTTA ACGAATACGACACGATTAGGG TTCGCTGTAAATGGCCATT (SEQ IDNO: 155) CCCA (SEQ ID NO: 156) Paenibacillus 127 128 F-C4AKA R-C4AKANN062253 TCACCATCATCCTAGGGCGG TTATTGATTAACGCGTCTA ACGAGTTCGACACGCTGCGTGATTCGCACTCGTCAGACG (SEQ ID NO: 157) CAGA (SEQ ID NO: 158) Microbacterium131 132 F-C3BXT R-C3BXT NN062175 TCACCATCATCCTAGGGCGATTATTGATTAACGCGTCTA CGATCACACAGGTCGCGGTGA CTGAACGACCACCCCCGT (SEQ ID NO:159) CGTG (SEQ ID NO: 160) Paenibacillus 135 136 F-C597E R-C597ENN062193 TCACCATCATCCTAGGGCCG TTATTGATTAACGCGTTTA TTCCGCCGCTGCCTGAAGGGAGTCACGCTAAT (SEQ ID NO: 161) (SEQ ID NO: 162) Paenibacillus 139140 F-C597F R-C597F NN062193 TCACCATCATCCTAGGGCCG TTATTGATTAACGCGTTTATTCCGCCGCTGCCT ATTCTCCAGCAGCAGCGC (SEQ ID NO: 163) (SEQ ID NO: 164)

Example 22 Cloning and Expression of a GH9 Gene from Microbacteriumtestaceum

A gene encoding a GH9 was found in the public database (DNA refEMBL:AP012052; SWISSPROT:E8N9Z4; SEQ ID NO:101 and SEQ ID NO 102respectively). A synthetic gene was amplified using specific oligos(table 29) and cloned and expressed in Bacillus subtilis with N-terminalpoly histidine tag (HHHHHHPR-) after the secretion signal as describedin examples 2 and 4. The nucleotide sequence of the fusion productcorresponds to SEQ ID NO: 103. The translated protein sequencecorresponds to SEQ ID NO: 104)

TABLE 29 Primers used for PCR amplification EQ ID NO SEQ ID NO of ofrecombinant poly- Specific Specific gene peptide primer forward primerreverse 103 104 F-C3FCE R-C3FCE TCACCATCATC TTATTGATTAA CTAGGGCAACCGCGTTTATTG AGTCAAACAA GACCAAAATG GTAGCAGTGT CCCGTCGTT (SEQ ID NO: (SEQID NO: 165) 166)

Example 23 Cloning and Expression of 2 GH9 Enzymes from Paenibacillussp-18054 and Paenibacillus sp-62408 in Bacillus subtilis

A linear integration vector-system was used for the expression cloningof the GH9 from Paenibacillus sp-18054 (SEQ ID NO: 85) and the GH9 fromPaenibacillus sp-62408 (SEQ ID NO: 89). The linear integration constructwas a PCR fusion product made by fusion of the gene between two Bacillussubtilis homologous chromosomal regions along with a strong promoter anda chloramphenicol resistance marker. The fusion was made by SOE PCR(Horton, R. M., Hunt, H. D., Ho, S. N., Pullen, J. K. and Pease, L. R.(1989), “Engineering hybrid genes without the use of restrictionenzymes, gene splicing by overlap extension”, Gene 77: 61-68). The SOEPCR method is also described in patent application WO 2003095658. Thegene was expressed under the control of a triple promoter system (asdescribed in WO 99/43835), consisting of the promoters from Bacilluslicheniformis alpha-amylase gene (amyL), Bacillus amyloliquefaciensalpha-amylase gene (amyQ), and the Bacillus thuringiensis cryIIIApromoter including stabilizing sequence. The gene coding forchloramphenicol acetyl-transferase was used as marker (described in e.g.Diderichsen, B.; Poulsen, G. B.; Joergensen, S. T., (1993), “A usefulcloning vector for Bacillus subtilis”, Plasmid, 30:312). The final geneconstructs were integrated on the Bacillus chromosome by homologousrecombination into the pectate lyase locus. The gene encoding the GH9from Paenibacillus sp-18054 was expressed as a truncated version (SEQ IDNO 87). The GH9 from Paenibacillus sp-62408 was expressed as a fulllength gene (SEQ ID NO 91). The gene fragments were amplified fromchromosomal DNA of the corresponding strains with gene specific primerscontaining overhang to the two flanking vector fragments (primersequences are listed in table 30). Both genes were expressed with aBacillus clausii secretion signal (with the following amino acidsequence: MKKPLGKIVASTALLISVAFSSSIASA) replacing the native secretionsignal and both genes were expressed with a poly histidine-tag (HHHHHH)linked to the C-terminal of the protein. A plasmid map of the linearvector with gene insert is shown in FIG. 1.

TABLE 30 Primers used for PCR amplification SEQ ID SEQ ID NO of NO ofAmplification recombinant poly- of GH9 gene gene peptide Specific primerforward Specific primer reverse Paenibacillus 87 88 D14KMG D14KMHsp-18054 GTTCATCGATCGCATCGGC TTAGTGGTGATGGTGATGATGGTC TGCTCCGGCTCCGCTGCGTCGAAGAACAGTGTTTGGGC (SEQ ID NO: 167) (SEQ ID NO: 168) Paenibacillus 9192 D14N38 D14N39 sp-62408 GTTCATCGATCGCATCGGC TTAGTGGTGATGGTGATGATGGTCTGCCACTCCCCCCTTGCC GGTTACCACTACGTCGTCAAAGA (SEQ ID NO: 169) (SEQ ID NO:170)

The 2 vector fragments and the gene fragment were subjected to aSplicing by Overlap Extension (SOE) PCR reaction to assemble the 3fragments into one linear vector construct. This was done independentlyfor each of the two genes. An aliquot of each of the two PCR productswas transformed into Bacillus subtilis. Transformants were selected onLB plates supplemented with 6 μg of chloramphenicol per ml. For eachconstruct a recombinant Bacillus subtilis clone containing theintegrated expression construct was grown in liquid culture. The enzymecontaining supernatants were harvested and the enzymes purified asdescribed in Example 5.

Example 24 Xanthan Degrading Activity of GH9 Enzymes and Xanthan Lyasesby Measurement of Viscosity Reduction

Viscosity measurements were carried out using different combinations ofxanthan lyases and GH9 endoglucanases as described in example 10. Theconcentration of the purified enzyme preparations used for the analysiswas 31.25 mg/L. Results presented are the average of three measurements.

TABLE 31 Viscosity measurements of different GH9's (SEQ ID NO: 6, 84,88, 92, 136, 140) and Xanthan Lyases (SEQ ID NO: 8, 108, 112, 116) onxantham gum T = T = 0 min T = 30 min T = 90 min 2 h 30 min T = 3 h 30min Average Average Average Average Average Sample (Pa) S.D (Pa) S.D(Pa) S.D (Pa) S.D (Pa) S.D Water 423 15 406 70 354 85 387 44 418 66Xanthan gum 0.25% 1140 69 1099 32 1011 98 1020 51 951 40 (control)Xanthan gum + 857 67 463 30 441 87 510 21 358 30 xanthan lyase (SEQ IDNO: 8) + GH9 (SEQ ID NO: 6) Xanthan gum + 960 36 533 131 368 31 490 25455 115 xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ ID NO: 84) Xanthan gum +1040 40 496 6 411 35 487 26 401 45 xanthan lyase (SEQ ID NO: 8) + GH9(SEQ ID NO: 88) Xanthan gum + 1013 71 659 25 458 46 490 23 361 38xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ ID NO: 92) Xanthan gum + 1060 20549 12 451 44 434 25 408 36 xanthan lyase (SEQ ID NO: 108) + GH9 (SEQ IDNO: 6) Xanthan gum + 1150 30 689 57 541 30 497 26 478 26 xanthan lyase(SEQ ID NO: 112) + GH9 (SEQ ID NO: 6) Xanthan gum + 1073 59 583 96 46859 484 31 391 51 xanthan lyase (SEQ ID NO: 116) + GH9 (SEQ ID NO: 6)Xanthan gum + 930 0 609 133 401 46 444 55 405 15 xanthan lyase (SEQ IDNO: 8) + GH9 (SEQ ID NO: 136) Xanthan gum + 1083 61 739 32 524 117 484 6401 55 xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ ID NO: 140)

TABLE 32 Viscosity measurements of a GH9 (SEQ ID NO: 88) and a XanthanLyase (SEQ ID NO: 120) on xantham gum T = 0 T = 30 min T = 1 hour T = 2hours T = 3 hours Average Average Average Average Average Sample (Pa)S.D (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D Water 496 60 606 32 457 29 459123 423 67 Xanthan gum 0.25% 1092 101 1112 76 1137 76 1089 32 1123 29(control) Xanthan gum + 946 61 626 45 587 45 486 17 430 40 xanthan lyase(SEQ ID NO: 120) + GH9 (SEQ ID NO: 88)

TABLE 33 Viscosity measurements of different GH9s (SEQ ID NO: 96, 100)and a Xanthan Lyase (SEQ ID NO: 68) on xantham gum T = 0 T = 1 hour T =2 hours T = 3 hours T = 4 hours Average Average Average Average AverageSample (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D Water 471 133 422 51411 68 431 134 422 32 Xanthan gum 0.5% 2048 151 2029 123 2098 121 211164 2076 55 (control) Xanthan gum + 1891 65 1465 76 1138 58 1078 59 98952 xanthan lyase (SEQ ID NO: 68) + GH9 (SEQ ID NO: 96) Xanthan gum +1685 81 602 29 538 25 548 45 579 104 xanthan lyase (SEQ ID NO: 68) + GH9(SEQ ID NO: 100)

TABLE 34 Viscosity measurements of a GH9 (SEQ ID NO: 88) and two XanthanLyases (SEQ ID NO: 124, 128) on xantham gum T = 0 T = 30 min T = 1 hourT = 2 hours T = 4 hours Average Average Average Average Average Sample(Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D Water 408 127 465 105 48425 423 21 365 32 Xanthan gum 0.5% 1848 86 1788 25 1780 78 1726 26 182555 (control) Xanthan gum + 2105 104 1691 21 1364 25 1246 135 779 17xanthan lyase (SEQ ID NO: 124) + GH9 (SEQ ID NO: 88) Xanthan gum + 1515191 678 70 520 6 469 76 572 32 xanthan lyase (SEQ ID NO: 128) + GH9 (SEQID NO: 88)

TABLE 35 Viscosity measurements of different GH9's (SEQ ID NO: 6, 58,104, 132) and Xanthan Lyases (SEQ ID NO: 8, 66, 124, 128) on xantham gumT = 0 T = 30 min T = 1 hour T = 2 hours T = 3 hours Average AverageAverage Average Average Sample (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D (Pa)S.D Water 444 40 474 125 377 56 520 52 423 75 Xanthan gum 0.25% 1374 311214 57 1217 62 1233 40 1280 25 Xanthan gum + 1231 78 871 75 687 0 72026 720 93 xanthan lyase (SEQ ID NO: 124) + GH9 (SEQ ID NO: 6) Xanthangum + 1124 75 721 92 633 118 693 146 563 26 xanthan lyase (SEQ ID NO:128) + GH9 (SEQ ID NO: 6) Xanthan gum + 1128 12 698 92 547 36 640 66 55091 xanthan lyase (SEQ ID NO: 124) + GH9 (SEQ ID NO: 58) Xanthan gum +1088 81 758 17 553 35 340 52 596 49 xanthan lyase (SEQ ID NO: 128) + GH9(SEQ ID NO: 58) Xanthan gum + 1184 57 921 67 877 79 683 45 713 40xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ ID NO: 104) Xanthan gum + 121161 784 64 623 32 767 6 580 12 xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ IDNO: 132) Xanthan gum + 1278 120 924 21 917 10 770 72 733 106 xanthanlyase (SEQ ID NO: 66) + GH9 (SEQ ID NO: 104) Xanthan gum + 1238 40 81846 623 12 807 172 613 82 xanthan lyase (SEQ ID NO: 66) + GH9 (SEQ ID NO:132)

TABLE 36 Viscosity measurements of different GH9's (SEQ ID NO: 136, 140)and a Xanthan Lyase (SEQ ID NO: 68) on xantham gum T = 0 T = 1 hour T =2 hours T = 3 hours T = 4 hours Average Average Average Average AverageSample (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D Water 471 133 422 51411 68 431 134 422 32 xanthan gum 0.5% 2048 151 2029 123 2098 121 211164 2076 55 (control) Xanthan gum + 1955 40 1242 29 911 35 771 32 609 70xanthan lyase (SEQ ID NO: 68) + GH9 (SEQ ID NO: 136) Xanthan gum + 176161 1375 50 931 29 775 10 699 36 xanthan lyase (SEQ ID NO: 68) + GH9 (SEQID NO: 140)

TABLE 37 Viscosity measurements of different GH9's (SEQ ID NO: 96, 100)and different Xanthan Lyases (SEQ ID NO: 8, 66) on xantham gum T = 0 T =30 min T = 1 hour T = 2 hours T = 4 hours Average Average AverageAverage Average Sample (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.D (Pa) S.DWater 420 55 415 15 490 62 384 20 409 55 Xanthan gum 0.25% 1320 125 123093 1195 46 1204 26 1174 42 Xanthan gum + 1184 56 695 110 575 107 739 138549 6 xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ ID NO: 96) Xanthan gum +1240 65 615 56 570 70 669 104 599 75 xanthan lyase (SEQ ID NO: 8) + GH9(SEQ ID NO: 100) Xanthan gum + 1244 111 610 178 680 82 704 131 654 20xanthan lyase (SEQ ID NO: 66) + GH9 (SEQ ID NO: 96) Xanthan gum + 124935 560 165 765 81 534 46 739 144 xanthan lyase (SEQ ID NO: 66) + GH9(SEQ ID NO: 100)

The results presented above show that all of the combinations of thedifferent GH9's and xanthan lyases tested can degrade the xanthanpresent in the media, thus leading to viscosity reduction.

Example 25 Colourmetric Assay of GH9 Endoglucanases on PretreatedXanthan Gum

GH9 endoglucanase activity was determined by reducing ends on xanthangum pre-treated with xanthan lyase using the colorimetric assaydeveloped by Lever (1972), Anal. Biochem. 47: 273-279, 1972. Anyreducing ends that are produced will react with PAHBAH generating anincrease of colour which is proportional to the enzyme activity underthe conditions used in the assay. Table 38 below shows the activity ofGH9 measured by the respective absorbance compared to that of thesubstrate alone.

Materials and Chemicals

0.1% Substrate: 6 ml (5 mg/ml) xanthan gum pre-treated with xanthanlyase in 24 ml Milli-Q water.

Activity buffer: 100 mM sodium acetate, 100 mM MES, 1 mM CaCl2, in 0.01%Triton X100, pH 7.

Ka—Na-tartrate/NaOH buffer: Dissolve Ka—Na-tartrate (50 g) and NaOH (20g) in water to a total volume of 1 liter. Store at 4° C.

Stop solution: Dissolve PAHBAH (Sigma H-9882) in Ka—Na-tartrate/NaOHsolution to a concentration of 15 mg/ml (e.g. dissolve 500 mg PAHBAH in33 ml Ka—Na-tartrate/NaOH solution)

Sample Preparation:

The enzyme samples were diluted to 0.1 mg/ml in activity buffer incostarstrips using a BioMek liquid handler robot. 50 μl of substrate and50 μl of each diluted sample was transferred to a 96-well PCR-MTP plate,50 μl activity buffer was added to each sample and the solutions mixed.The sealed PCR-plate was incubated in a PCR machine at 37° C. for 15min. then immediately cooled to 10° C. 75 μl of the stop solution wasadded to each sample, the mixture was shaken, and 75 μl of each samplewas discarded. The samples were incubated for 10 min. at 95° C., then 1min. 10° C. 150 μl of each sample was transferred to a new 96-wellPCR-MTP and the absorbance at 405 nm was measured.

TABLE 38 Colourmetric reducinq ends assay of different GH9s on xanthangum pre-treated with xanthan lyase GH9 endoglucanase mAU (pH 7) Blank0.21 SEQ ID NO: 6 1.25 SEQ ID NO: 58 1.26 SEQ ID NO: 92 1.09 SEQ ID NO:100 1.18

The data shows that the reaction of xanthan gum pre-treated with xanthanlyase with a GH9 endoglucanase results in a stronger colourmetricresponse. Since the colourmetric response is proportional to the amountof reducing ends produced, then it can clearly be seen that the GH9endoglucanases have activity on xanthan gum pre-treated with xanthanlyase.

Example 26 Colourmetric Assay of Xanthan Lyases on Xanthan Gum

Xanthan lyase activity was determined by reducing ends as described inexample 25, except that 0.1% xanthan gum was used as substrate. Theresults are presented in table 39 below.

TABLE 39 Colourmetric reducing ends assay of different xanthan lyases onxanthan gum. Xanthan Lyase mAU (pH 7) Blank 0.21 SEQ ID NO: 8 0.65 SEQID NO: 120 0.46 SEQ ID NO: 68 0.63 SEQ ID NO: 116 0.65 SEQ ID NO: 1120.66 SEQ ID NO: 108 0.48 SEQ ID NO: 66 0.44

The data shows that the reaction of xanthan gum with a xanthan lyaseresults in a stronger colourmetric response and therefore the xanthanlyases have activity on xanthan gum.

Example 27 Colourmetric Assay of Xanthan Lyases and GH9 Engoglucanaseson Xanthan Gum

Xanthan lyase activity alone and together with a GH9 endoglucanase wasdetermined by reducing ends as described in example 25, except that 0.1%xanthan gum was used as substrate. The results are presented in tables40 and 41 below.

TABLE 40 Colourmetric reducina ends assay of different xanthan lyasesalone or incombination with a GH9 endoqlucanase on xanthan gum mAU (pH7) of mAU (pH 7) of xanthan lyase + xanthan GH9 endoglucanase XanthanLyase lyase alone (SEQ ID NO: 6) Blank 0.14 0.15 Xanthan lyase (SEQ IDNO: 8) 0.61 2.06 Xanthan lyase (SEQ ID NO: 112) 0.51 1.91 Xanthan lyase(SEQ ID NO: 124) 0.42 1.91 Xanthan lyase (SEQ ID NO: 128) 0.43 1.85

TABLE 40 Relative response of colourmetric reducing ends assay ofdifferent xanthan lyases alone or incombination with a GH9 endoglucanaseon xanthan gum Relative Relative response response of of xanthan lyase +xanthan GH9 endoglucanase Xanthan Lyase lyase alone (SEQ ID NO: 6) Blank23 25 Xanthan lyase (SEQ ID NO: 8) 100 337 Xanthan lyase (SEQ ID NO:112) 84 312 Xanthan lyase (SEQ ID NO: 124) 69 312 Xanthan lyase (SEQ IDNO: 128) 71 302

Responses are set relative to the response of xanthan lyase of SEQ IDNO: 8 which is set to 100.

The data shows that the reaction of xanthan gum with a xanthan lyaseresults in a significantly stronger colourmetric response and thereforethe xanthan lyases alone have significant activity on xanthan gum.Furthermore, addition of the GH9 endoglucanase of SEQ ID NO: 6 resultsin at least a 3-4 fold increase in colourmetric response over the use ofthe xanthan lyase alone, showing that use of the two enzymes togetherresults in a synergistic degradation of xanthan gum.

Example 28 MiniLOM Wash Performance of Xanthan Lyase (SEQ ID NO:) and/orGH9 (SEQ ID NO:)

The enzymes of the present invention were tested using the miniLOM assayin order to determine the “enzyme detergency effect”. Test tubes arefilled with test solution, soiled fabrics and steel balls and rotated ina heating cabinet at a given temperature. Cleaning benefits are studiedwhen washing in model liquid detergent A. The experimental conditionsfor the experiments are specified in Table 41.

TABLE 41 Experimental conditions for MiniLOM Test solution Modeldetergent A Test solution volume 40 mL pH Not adjusted Wash time 30minutes Temperature 40° C. Water hardness 16° dH Enzyme dosage Xanthanlyase: 1 mg EP/L GH9: 0.5 mg EP/L Ca²⁺:Mg²⁺:CO₃ ²⁻ ratio 5:1:3 SwatchesCircular swatches 2 cm in diameter Stains 4 × DN31C (Half amount ofxanthan gum/carbon black); 4 × DN31D (Xanthan gum/carbon black) Ballast4 × wfk10A (100% woven cotton) 4 × wfk80A (100% knitted cotton)Mechanics 5 stainless steel balls, 6 mm in diameter

Water hardness was adjusted by addition of CaCl₂, MgCl₂, and NaHCO₃ tothe test system. After washing the textiles were flushed in tap waterand air-dried. The swatches were prepared by adding xanthan gum fromXanthomonas campestris (Food Grade Keltrol T, Kelco) mixed with carbonblack to a cotton fabric. The DN31C swatch is prepared with half theamount of xanthan gum; otherwise it is identical to the DN31D swatch.However, this does have the effect of reducing the measurement windowfor enzymatic effects, in that the amount of xanthan gum which may beremoved is reduced. In effect, this leads to a smaller increase inintensity when compared to the detergent alone effects, but should notbe construed as a lesser enzymatic effect.

The performance of the enzyme(s) is evaluated by measuring the remissionof the textile swatches using the ColorEye at 460 nm. The results usingswatch C are presented in tables 42 and 43, whilst the results usingswatch D are presented in tables 44 and 45.

Remission Measured Before Wash:

Swatch DN31C: 28.87±0.37

Swatch DN31D: 29.34±0.66

Remission Measured Using Detergent Only:

Swatch DN31C: 35.37±1.00

Swatch DN31D: 39.79±1.28

TABLE 42 Remission (460 nm) values of MimiLOM wash using 6 different GH9endoglucanases and 6 different xanthan lyases on swatch DN31C XanthanLyase Rem₄₆₀ SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID GH9 endoglucanaseNO: 8 NO: 66 NO: 108 NO: 112 NO: 116 NO: 120 SEQ ID NO: 6 42.17 43.0741.70 43.00 42.05 42.39 SEQ ID NO: 84 37.06 39.06 38.19 38.48 37.56 —SEQ ID NO: 88 37.29 39.46 38.18 38.80 39.62 37.00 SEQ ID NO: 92 38.9040.21 39.27 40.01 38.89 — SEQ ID NO: 96 37.00 38.68 36.92 37.32 — — SEQID NO: 100 36.33 38.45 37.63 37.60 36.39 36.91

TABLE 43 Standard Deviation of MimiLOM results on swatch DN31C XanthanLyase Standard deviation SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID GH9endoglucanase NO: 8 NO: 66 NO: 108 NO: 112 NO: 116 NO: 120 SEQ ID NO: 60.80 0.49 0.64 0.30 0.43 0.61 SEQ ID NO: 84 0.79 0.55 0.98 0.91 1.06 —SEQ ID NO: 88 0.73 0.53 0.91 0.49 0.30 0.62 SEQ ID NO: 92 0.85 0.50 0.840.72 0.61 — SEQ ID NO: 96 1.20 1.48 0.69 0.96 — — SEQ ID NO: 100 0.700.51 0.83 0.90 0.70 0.74

The results show that the GH9 endoglucanases of SEQ ID NO: 6, 84, 88 and92 give a statistically significant wash performance according to theANOVA tukey test on swatch DN31C together with the xanthan lyases of SEQID NO: 8, 66, 108, 112, 116 and 120 in all cases. Furthermore, the GH9endoglucanases of SEQ ID NO: 100 showed a statistically significant washperformance with the xanthan lyases of SEQ ID NO: 66, 108, 112 and 120and at least a numerically improved wash performance with the xanthanlyases of SEQ ID NO: 8 and 116.

TABLE 44 Remission (460 nm) values of MimiLOM wash using 6 different GH9endoglucanases and 6 different xanthan lyases on swatch DN31D XanthanLyase Rem₄₆₀ SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID GH9 endoglucanaseNO: 8 NO: 66 NO: 108 NO: 112 NO: 116 NO: 120 SEQ ID NO: 6 48.79 49.3647.72 49.02 48.28 48.78 SEQ ID NO: 84 41.98 42.66 43.01 43.16 42.24 —SEQ ID NO: 88 41.72 43.67 42.56 42.94 43.25 42.65 SEQ ID NO: 92 43.5944.15 44.20 44.88 43.84 — SEQ ID NO: 96 40.98 41.25 41.49 41.17 — — SEQID NO: 100 40.88 42.13 41.83 42.28 41.46 41.43

TABLE 45 Standard Deviation of MimiLOM results on swatch DN31D XanthanLyase Standard deviation SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID GH9endoglucanase NO: 8 NO: 66 NO: 108 NO: 112 NO: 116 NO: 120 SEQ ID NO: 61.14 0.66 0.60 0.44 0.29 0.41 SEQ ID NO: 84 1.18 0.68 1.55 1.65 1.79 —SEQ ID NO: 88 1.28 0.49 1.93 1.85 0.33 1.75 SEQ ID NO: 92 1.66 0.30 1.231.50 1.13 — SEQ ID NO: 96 1.45 1.26 1.02 1.67 — — SEQ ID NO: 100 1.080.74 1.46 1.42 1.47 0.73

The results show that the GH9 endoglucanases of SEQ ID NO: 6, 84 and 92showed a statistically significant wash performance according to theANOVA tukey test on swatch DN31D together with the xanthan lyases of SEQID NO: 8, 66, 108, 112, 116 and 120 in all cases. Furthermore, the GH9endoglucanase of SEQ ID NO: 88 showed a statistically significant washperformance with the xanthan lyases of SEQ ID NO: 66, 108, 112, 116 and120 and a numerically improved wash performance with the xanthan lyaseof SEQ ID NO: 8. The GH9 endoglucanase of SEQ ID NO: 100 showed astatistically significant wash performance with the xanthan lyases ofSEQ ID NO: 66, 108 and 112 and a numerically improved wash performancewith the other 3 xanthan lyases. The GH9 endoglucanases of SEQ ID NO: 96showed a numerically improved wash performance together with all of thexanthan lyases tested.

Example 29 Xanthan Degrading Activity of GH9 Endoglucanases and XanthanLyases by Measurement of Viscosity Reduction

Viscosity measurements were carried as described in example 10 on twodifferent batches of the GH9 endoglucanase of SEQ ID NO: 6 and a singlebatch of the GH9 endoglucanase of SEQ ID NO: 2 together with twodifferent xanthan lyases (SEQ ID NO: 8 and 66). SEQ ID NO: 6 isidentical to SEQ ID NO: 2 except that it contains a His-tag (i.e.-RPHHHHHH) attached to the N-terminal of the mature polypeptide. Theconcentration of the purified enzyme preparations used for the analysiswas 31.25 mg/L. Results presented are the average of three measurementsand are shown in table 46 below.

TABLE 46 Viscosity measurements of the same GH9 with and without His-tag(SEQ ID NO: 2, 6) and two different xanthan lyases (SEQ ID NO: 8, 66) onxantham gum T = 0 T = 30 min T = 1 hour T = 2 hours T = 4 hours AverageAverage Average Average Average Sample (Pa) S.D (Pa) S.D (Pa) S.D (Pa)S.D (Pa) S.D Water 400 10 441 44 420 21 410 0 518 124 Xanthan gum 0.5%1106 81 1144 50 1196 55 1123 58 1075 40 (control) Xanthan gum + 890 26624 85 543 56 567 38 561 35 xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ IDNO: 6)* Xanthan gum + 986 55 577 40 586 75 523 23 525 46 xanthan lyase(SEQ ID NO: 8) + GH9 (SEQ ID NO: 2) Xanthan gum + 1030 72 644 75 626 175547 21 565 72 xanthan lyase (SEQ ID NO: 8) + GH9 (SEQ ID NO: 6)**Xanthan gum + 986 108 604 80 563 62 650 72 525 61 xanthan lyase (SEQ IDNO: 66) + GH9 (SEQ ID NO: 6)* Xanthan gum + 1093 95 611 75 606 98 593 50601 21 xanthan lyase (SEQ ID NO: 66) + GH9 (SEQ ID NO: 2) Xanthan gum +1080 56 557 31 580 40 597 90 628 108 xanthan lyase (SEQ ID NO: 66) + GH9(SEQ ID NO: 6)** *batch 1; **batch 2

The results in table 46 show that there is no significant difference inthe drop in viscosity between the two batches of the GH9 endoglucanaseof SEQ ID NO: 6 which has a His-tag and the GH9 endoglucanase of SEQ IDNO: 2 which is without the His-tag together with either xanthan lyase.It can therefore be concluded that the His-tag does not alter thexanthan gum degrading properties of the GH9 endoglucanase of SEQ ID NO:2.

Example 30 Colourmetric Assay of GH9 Endoglucanases and Xanthan Lyaseson Xanthan Gum

The activity of GH9 endoglucanases alone and in combination withdifferent xanthan lyases on xanthan gum was determined by reducing endsas described in example 25, except that 0.1% xanthan gum was used assubstrate. The results are presented in table 47 below.

TABLE 47 Colourmetric reducing ends assay of different GH9endoglucanases (SEQ ID NO: 2, 6, 16, 58, 84, 92, 96 and 100) and xanthanlyases (SEQ ID NO: 8, 66, 68, 120) on xanthan gum. mAU GH9 endoglucanase(pH 7) SEQ SEQ SEQ SEQ SEQ SEQ SEQ SEQ SEQ SEQ ID: Xanthan ID NO: ID NO:ID NO: ID NO: ID NO: ID NO: ID NO: ID NO: ID NO: NO: Lyase 6* 6** 2 1658 84 88 92 96 100 SEQ ID 1.75 1.53 1.62 1.54 2.28 2.22 1.70 1.84 1.451.86 NO: 8 SEQ ID 1.78 1.58 1.84 1.69 1.88 2.16 1.86 1.77 1.46 1.96 NO:66 SEQ ID 2.08 1.92 1.87 1.93 2.22 2.10 2.02 1.79 1.53 1.88 NO: 68 SEQID 1.04 1.05 1.08 0.91 1.62 1.73 1.40 1.35 0.95 1.42 NO: 120 None 0.470.42 0.45 0.25 0.77 0.66 0.26 0.24 0.27 0.30 *batch 1; **batch 2

The results demonstrate that all of the GH9 endoglucanases together withall of the xanthan lyases tested give a significant increase incolourmetric response showing that the combination of these GH9endoglucanases and xanthan lyases has significant activity on degradingxanthan gum. The results further show that there is no significantdifference between the two batches of the GH9 endoglucanase of SEQ IDNO: 6 tested, nor that the His-tag which is present on the GH9endoglucanase of SEQ ID NO: 6 results in any significant change inperformance over the corresponding GH9 endoglucanase without His-tag(SEQ ID NO: 2).

Example 31 AMSA Wash Performance of Xanthan Lyases and GH9Endoglucanases

The experiments were conducted as described in the Automatic MechanicalStress Assay (AMSA) for laundry method using a single cycle washprocedure and the experimental conditions specified in table 48 below.The results are given in tables 49 and 50 using 3 different GH9endoglucanases and 6 different xanthan lyases along with controls whereeither the GH9 endoglucanase and/or xanthan lyase are absent. Theresults are shown as the ΔInt enzyme value.

TABLE 48 Experimental conditions for Wash Cycle Test solution 3.33 g/LModel liquid detergent B Test solution volume 140 μL detergent per slot;20 μL enzyme per slot pH Unadjusted Wash time 20 minutes Temperature 20°C. or 40° C. Enzyme dosage Xanthan lyase: 1 mg EP/L GH9: 0.5 mg EP/LWater hardness 15° dH Ca²⁺:Mg²⁺:CO₃ ²⁻ ratio 5:1:3 Swatch DN31C (Halfamount of xanthan gum with carbon black)

Water hardness was adjusted by addition of CaCl₂, MgCl₂, and NaHCO₃ tothe test system. After washing the textiles were flushed in tap waterand air-dried. The swatches were prepared by adding xanthan gum fromXanthomonas campestris (Food Grade Keltrol T, Kelco) mixed with carbonblack to a cotton fabric. The DN31C swatch is prepared with half theamount of xanthan gum; otherwise it is identical to the DN31D swatch.However, this does have the effect of reducing the measurement windowfor enzymatic effects, in that the amount of xanthan gum which may beremoved is reduced. In effect, this leads to a smaller increase inintensity when compared to the detergent alone effects, but should notbe construed as a lesser enzymatic effect.

TABLE 49 AMSA wash data using model liquid detergent B at 20° C. onswatch DN31C ΔInt enzyme GH9 endoglucanase value. SEQ SEQ Xanthan LyaseControl ID NO: 6 SEQ ID NO: 88 ID NO: 100 Control 0.0 5.9 2.9 2.0 SEQ IDNO: 8 5.0 16.3 6.4 0.9 SEQ ID NO: 66 2.5 14.4 6.6 3.5 SEQ ID NO: 108−0.2 10.8 — — SEQ ID NO: 116 5.6 12.0 — — SEQ ID NO: 124 −0.4 8.5 — —SEQ ID NO: 128 4.6 13.1 — —

TABLE 50 AMSA wash data using model liquid detergent B at 40° C. onswatch DN31C ΔInt enzyme GH9 endoglucanase value. SEQ SEQ Xanthan LyaseControl ID NO: 6 SEQ ID NO: 88 ID NO: 100 Control 0.0 7.3 3.3 3.7 SEQ IDNO: 8 4.8 16.1 8.0 3.0 SEQ ID NO: 66 2.2 16.2 9.3 6.1 SEQ ID NO: 108−3.7 9.7 — — SEQ ID NO: 116 6.2 12.0 — — SEQ ID NO: 124 1.0 10.1 — — SEQID NO: 128 6.8 13.3 — —

The data shows that the GH9 endoglucanase of SEQ ID NO: 6 gives asignificant wash effect with all of the xanthan lyases (i.e. SEQ ID NO:8, 66, 108, 116, 124 and 128) tested at both 20° C. and 40° C.Furthermore, the GH9 endoglucanase of SEQ ID NO: 88 give a significantwash effect with both xanthan lyases tested, and a significantsynergistic effect together with the xanthan lyase of SEQ ID NO: 66. TheGH9 endoglucanase of SEQ ID NO: 100 shows a significant wash effect withthe xanthan lyase of SEQ ID NO: 66 at both 20° C. and 40° C.

Example 32 MiniLOM Wash Performance of GH9 Endoglucanase

The GH9 endoglucanases were tested using the miniLOM assay in order todetermine the enzyme detergency benefit of the GH9 endoglucanase. Theenzyme detergency benefit was studied by comparing the wash effect onxanthan gum with carbon black stains with and without a GH9endoglucanase in either buffer (2-(N-morpholino)ethanesulfonic acid,MES), or model detergent A using the conditions described in table 51.The results for stain DN31C are given in tables 52 and 53 and for stainDN31D are given in tables 54 and 55.

TABLE 51 MiniLOM Wash Conditions Test solution Buffer (50 mM MES) orModel Detergent A (3.33 g/L) Test solution volume 40 mL pH Adjusted topH 7.0 (buffer) or pH 7.2 (Model Detergent A) prior to wash Wash time 30minutes Temperature 40° C. Water hardness 16° dH Ca²⁺:Mg²⁺:CO₃ ²⁻ ratio5:1:3 Swatches Circular swatches 2 cm in diameter 8 x Technical stainswith Xanthan Gum with Stains Carbon Black. Stain DN31D has 2x xanthangum compared to DN31C. Ballast 4 × wfk10A (100% woven cotton) 4 × wfk80A(100% knitted cotton) Total ballast weight Technical stains: 0.43 g pertube Ballast stains: 0.53 g per tube Mechanics 5 stainless steel balls,6 mm in diameter

Water hardness was adjusted by addition of CaCl₂, MgCl₂, and NaHCO₃ tothe test system. After washing, the textiles were flushed in tap waterand air-dried. The swatches were prepared by applying a mixture ofcarbon black (0.05-0.06 g) and xanthan gum (1.2-1.4 g for DN31C, 2.4-2.6g for DN31D, Xanthomonas campestris (Food Grade Keltrol T, Kelco) persquare meter of cotton fabric. The enzyme detergency benefit of theenzyme(s) was evaluated by measuring the remission of the textileswatches using the ColorEye at 460 nm as described in the Evaluation ofStains.

TABLE 52 Results of GH9 Endoglucanse (SEQ ID NO: 6) on XanthanGum/Carbon Black Stains (DN31C) GH9 Buffer (50 mM MES) Model Detergent A(mg/L) REM (460 nm) Std. Dev. REM (460 nm) Std. Dev. 0 34.5 0.6 36.8 2.90.2 40.3 0.2 41.1 0.3 0.4 39.6 0.3 41.1 0.7 0.8 40.4 0.4 41.0 0.4

TABLE 53 Results of GH9 Endoglucanse (SEQ ID NO: 6) on XanthanGum/Carbon Black Stains (DN31C) GH9 Buffer (50 mM MES) Model Detergent A(mg/L) REM (460 nm) Std. Dev. REM (460 nm) Std. Dev. 0 35.4 0.5 36.7 0.30.05 39.6 0.9 39.1 2.8 0.1 39.3 1.0 40.6 0.5 0.2 39.8 0.4 40.9 0.3 0.540.0 0.3 40.9 0.4 0.5 ppm BSA¹ 35.4 0.2 35.8 0.1 ¹BSA—Bovine serumalbumine added instead of GH9 endoglucanase

TABLE 54 Results of GH9 Endoglucanse (SEQ ID NO: 6) on XanthanGum/Carbon Black Stains (DN31D) GH9 Buffer (50 mM MES) Model Detergent A(mg/L) REM (460 nm) Std. Dev. REM (460 nm) Std. Dev. 0 39.8 0.7 40.9 1.70.2 47.2 0.3 47.6 0.4 0.4 46.5 0.4 47.6 0.4 0.8 46.8 0.4 48.0 0.6

TABLE 55 Results of GH9 Endoglucanse (SEQ ID NO: 6) on XanthanGum/Carbon Black Stains (DN31D) GH9 Buffer (50 mM MES) Model Detergent A(mg/L) REM (460 nm) Std. Dev. REM (460 nm) Std. Dev. 0 40.2 0.9 41.6 0.40.05 46.2 0.8 45.3 4.1 0.1 45.8 0.7 47.3 0.9 0.2 46.4 0.4 47.8 0.8 0.546.6 1.0 48.0 1.1 0.5 ppm BSA¹ 39.4 0.3 41.4 0.8 ¹BSA—Bovine serumalbumine added instead of GH9 endoglucanase

The results showed that there was significant enzyme detergency, stainremoval and cleaning benefits when the GH9 endoglucanase (SEQ ID NO: 6)was added to the wash solution using either buffer (50 mM MES) or withmodel detergent A. Tables 52 and 54 show that the same enzyme detergencybenefit was observed when between 0.2 and 0.8 mg enzyme protein per Lwash liquor was used, indicating that a plateau level may already havebe reached when dosing above 0.2 mg EP/L.

Repeating the experiment using lower amounts of endoglucanase (SEQ IDNO: 6) (tables 53 and 55) showed that significant enzyme detergencybenefit was apparent even at 0.05 mg enzyme protein per L wash liquor.The addition of 0.5 ppm bovine serum albumine instead of the GH9endoglucanase showed that the enzyme detergency benefit was not due toan unspecific protein effect.

The largest effect can be seen on stain DN31D where benefits of up to 7delta REM units were found when using either buffer (50 mM MES) or withmodel detergent A.

Example 33 Effects of GH9 Endoglucanase on (Pre-Treated) Xanthan Gum asDetermined by Viscosity Reduction

0.5% pre-treated xanthan gum was prepared by pre-treating the xanthangum with xanthan lyase as described in Nankai, H., Hashimoto, W., Miki,H., Kawai, S., and Murata, K. (1999) “Microbial system forpolysaccharide depolymerization: Enzymatic route for xanthandepolymerization by bacillus sp strain gl1”, Applied and EnvironmentalMicrobiology 65, 2520-2526. Prior to use all enzymes were buffer changedto the MES buffer using NAP 5 columns (GE Healthcare).

The samples were hydrolysed using the following conditions: 0.25%xanthan gum or 0.5% pre-treated xanthan gum in 50 mM MES buffer+0.01%triton x-100 at pH 7.0 and 40° C.

The initial viscosity was measured upon thermal equilibration and priorto enzyme addition using the ViPr assay. After thermal equilibration,the GH9 endoglucanase (SEQ ID NO: 6) (20 mg/L), if appropriate, wasadded and the viscosity was then measured at various time points. Thedata is presented in table 56 below.

TABLE 56 Results of GH9 Endoglucanse (SEQ ID NO: 6) on Xanthan Gum andPre-treated Xanthan Gum as determined by Viscosity Reduction IncubationTime 0 min 5 min 15 min 30 min 3 hous Std Std Std Std Std MeasurementsMean Dev Mean Dev Mean Dev Mean Dev Mean Dev Conditions Pa ± Pa ± Pa ±Pa ± Pa ± Buffer 515 15 558 15 524 82 560 68 517 42 (control, no enzyme)Xanthan gum 1148 32 1146 32 1174 10 1136 12 1077 45 (control, no enzyme)Xanthan gum + 1042 17 903 17 867 6 846 38 837 55 GH 9 (SEQ ID NO: 6)Pre-treated Xanthan 1135 120 1206 120 1314 0 1223 71 1247 46 gum(control, no enzyme) Pre-treated Xanthan 1025 15 629 15 661 70 553 49544 30 gum + GH 9 (SEQ ID NO: 6)

The buffer control represents the viscosity representative of completehydrolysis. At this point there are little to no solvent-polymerinteractions which would lead to an increase in solvent viscosity. Thexanthan gum and modified xanthan gum controls remain constant throughoutthe incubation displaying the robustness of the assay. The GH9endoglucanase (SEQ ID NO: 6) is seen to decrease the xanthan gumsubstrate over the course of the 3 h incubation but the viscosity doesnot reach the viscosity of the control. The xanthan lyase pretreatedxanthan gum is reduced to the buffer viscosity almost immediately underthese conditions by the GH9 endoglucanase (SEQ ID NO: 6).

Example 34 Effects of GH9 Endoglucanase on (Pre-Treated) Xanthan Gum asDetermined by Reducing Ends

0.25% pre-treated xanthan gum was prepared by pre-treating the xanthangum with xanthan lyase as described in example 33. Prior to use allenzymes were buffer changed to the MES buffer using NAP 5 columns (GEHealthcare). The samples were hydrolysed using the following conditions:0.25% xanthan gum or 0.25% pre-treated xanthan gum in 50 mM MESbuffer+0.01% triton x-100 at pH 7.0 and 30° C.

After thermal equilibration, the GH9 endoglucanase (SEQ ID NO: 6) (62mg/L), if appropriate, was added and the produced reducing ends weremeasured at the end point using the BCA Reducing Ends assay.Quantification of reducing ends was based on a glucose standard curveand the results are shown in table 57 below.

TABLE 57 Results of GH9 Endoglucanse (SEQ ID NO: 6) on Xanthan Gum andPre-treated Xanthan Gum as determined by Reducing Ends BCA at 30 minIncubation Time Standard Measurements Average deviation Conditions μMglucose equivalents ± Buffer (control, no enzyme) 0 0 Xanthan gum 173 5(control, no enzyme) Xanthan gum + GH 9 (SEQ ID 177 5 NO: 6) Pre-treatedXanthan gum 534 21 (control, no enzyme) Pre-treated Xanthan gum + GH 92367 455 (SEQ ID NO: 6)

What is claimed is:
 1. A recombinant host cell comprising an expressionvector comprising a polynucleotide encoding a GH9 endoglucanase, wherein(a) the GH9 endoglucanase has at least 90% sequence identity to aminoacids 1 to 1055 of SEQ ID NO: 2; and (b) the polynucleotide is operablylinked to one or more control sequences that direct the production ofthe polypeptide.
 2. The recombinant host cell of claim 1, wherein theGH9 endoglucanase has at least 92% sequence identity to amino acids 1 to1055 of SEQ ID NO:
 2. 3. The recombinant host cell of claim 1, whereinthe GH9 endoglucanase has at least 94% sequence identity to amino acids1 to 1055 of SEQ ID NO:
 2. 4. The recombinant host cell of claim 1,wherein the GH9 endoglucanase has at least 95% sequence identity toamino acids 1 to 1055 of SEQ ID NO:
 2. 5. The recombinant host cell ofclaim 1, wherein the GH9 endoglucanase has at least 97% sequenceidentity to amino acids 1 to 1055 of SEQ ID NO:
 2. 6. The recombinanthost cell of claim 1, wherein the GH9 endoglucanase has at least 98%sequence identity to amino acids 1 to 1055 of SEQ ID NO:
 2. 7. Therecombinant host cell of claim 1, wherein the GH9 endoglucanase has atleast 99% sequence identity to amino acids 1 to 1055 of SEQ ID NO:
 2. 8.The recombinant host cell of claim 1, wherein the GH9 endoglucanase is afragment of amino acids 1 to 1055 of SEQ ID NO: 2, wherein the fragmenthas activity on xanthan gum pretreated with xanthan lyase, xanthandegrading activity and/or endo-β-1,4-glucanase activity.
 9. Therecombinant host cell of claim 1, wherein the one or more controlsequences comprise a foreign control sequence.
 10. A method of producinga GH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 1 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 11. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 2 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 12. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 3 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 13. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 4 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 14. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 5 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 15. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 6 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 16. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 7 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 17. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 8 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 18. A method of producing aGH9 endoglucanase, comprising (a) culturing a recombinant host cell ofclaim 9 under conditions conducive for producing the GH9 endoglucanase;and (b) recovering the GH9 endoglucanase.
 19. A method for degradingxanthan gum comprising applying a GH9 endoglucanase having at least 90%sequence identity to amino acids 1 to 1055 of SEQ ID NO: 2 to thexanthum gum, wherein the xanthan gum is on the surface of a textile,hard surface or is a component in a borehole filtercake.
 20. The methodof claim 19, wherein the GH9 polypeptide has at least 95% sequenceidentity to amino acids 1 to 1055 of SEQ ID NO: 2.